CAZypedia - User contributions [en-ca]

Carbohydrate Binding Module Family 20

2019-12-15T19:54:10Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 modules bind starch granules (raw starch), its soluble components amylose and amylopectin as well as derived maltooligosaccharides (maltose, maltoheptaose, maltodecaose). Furthermore ɑ-, β-, and γ-cyclodextrin, which mimic amylose, have been used for studying CBM20-carbohydrate binding. An overview of ligand specificities and affinities of specific CBM20s can be found in <cite>Christiansen2009</cite>. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [{{PDBlink}}1ac0 1AC0] <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

The CBM20 members are type B CBMs and their overall fold is a β-sandwich (Fig. 1). At least one but more typically two binding sites have been found in determined structures having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 cyclodextrin glucanotransferase (CGTase) from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin (Fig. 1) <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 
== Functionalities ==

The CBM20 from the A. niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from [[GH77]], but can also belong to [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from A. awamori <cite>Hayashida1982</cite> and A. niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans 8 (PDB entry [{{PDBlink}}1cgt 1CGT]) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the structure of the [[GH13]] CGTase from Bacillus circulans 251 (PDB entry [{{PDBlink}}1cdg 1CDG]) <cite>Lawson1994</cite>.


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
#Lawson1994 pmid=8107143

#Christiansen2009 pmid=19682075

</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-12-15T19:23:05Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 modules bind starch granules (raw starch), its soluble components amylose and amylopectin as well as derived maltooligosaccharides (maltose, maltoheptaose, maltodecaose). Furthermore ɑ-, β-, and γ-cyclodextrin, which mimic amylose, have been used for studying CBM20-carbohydrate binding. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [{{PDBlink}}1ac0 1AC0] <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

The CBM20 members are type B CBMs and their overall fold is a β-sandwich (Fig. 1). At least one but more typically two binding sites have been found in determined structures having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 cyclodextrin glucanotransferase (CGTase) from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin (Fig. 1) <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 
== Functionalities ==

The CBM20 from the A. niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from [[GH77]], but can also belong to [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from A. awamori <cite>Hayashida1982</cite> and A. niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans 8 (PDB entry [{{PDBlink}}1cgt 1CGT]) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the structure of the [[GH13]] CGTase from Bacillus circulans 251 (PDB entry [{{PDBlink}}1cdg 1CDG]) <cite>Lawson1994</cite>.


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
#Lawson1994 pmid=8107143
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-12-15T18:45:07Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 modules bind starch granules (raw starch), its soluble components amylose and amylopectin as well as derived maltooligosaccharides (maltose, maltoheptaose, maltodecaose). Furthermore ɑ-, β-, and γ-cyclodextrin, which mimic amylose, have been used for studying CBM20-carbohydrate binding. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [{{PDBlink}}1ac0 1AC0] <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

The CBM20 members are type B CBMs and their overall fold is a β-sandwich (Fig. 1). At least one but more typically two binding sites have been found in determined structures having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 cyclodextrin glucanotransferase (CGTase) from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin (Fig. 1) <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 
== Functionalities ==

The CBM20 from the A. niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from [[GH77]], but can also belong to [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from A. awamori <cite>Hayashida1982</cite> and A. niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry [{{PDBlink}}1cgt 1CGT]) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-12-15T18:31:03Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 modules bind starch granules (raw starch), its soluble components amylose and amylopectin as well as derived maltooligosaccharides (maltose, maltoheptaose, maltodecaose). Furthermore ɑ-, β-, and γ-cyclodextrin, which mimic amylose, have been used for studying CBM20-carbohydrate binding. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [{{PDBlink}}1ac0 1AC0] <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

The CBM20 members are type B CBMs and their overall fold is a β-sandwich (Fig. 1). At least one but more typically two binding sites have been found in determined structures having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 
== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry [{{PDBlink}}1cgt 1CGT]) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-12-15T18:28:54Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 modules bind starch granules (raw starch), its soluble components amylose and amylopectin as well as derived maltooligosaccharides (maltose, maltoheptaose, maltodecaose). Furthermore as ɑ-, β-, and γ-cyclodextrin, which mimic amylose, have been used for studying CBM20-carbohydrate binding. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [{{PDBlink}}1ac0 1AC0] <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

The CBM20 members are type B CBMs and their overall fold is a β-sandwich. At least one but more typically two binding sites have been found in determined structures having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 
== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry [{{PDBlink}}1cgt 1CGT]) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-15T13:55:27Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch), its soluble components amylose and amylopectin as well as derived maltooligosaccharides (maltose, maltoheptaose, maltodecaose). Furthermore as ɑ-, β-, and γ-cyclodextrin, which mimic amylose, have been used for studying CBM20-carbohydrate binding. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [https://www.rcsb.org/structure/1ac0 1AC0]; <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry 1CGT) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-15T13:48:49Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch), its soluble components amylose and amylopectin as well as β-cyclodextrin, a small amylose mimicing cyclic carbohydrate. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [https://www.rcsb.org/structure/1ac0 1AC0]; <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry 1CGT) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-15T13:46:11Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch), its soluble components amylose and amylopectin as well as β-cyclodextrin, a small amylose mimicing cyclic carbohydrate. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with β-cyclodextrin bound to both binding sites (PDB ID [https://www.rcsb.org/structure/1ac0 1AC0]; <cite>Sorimachi1997</cite>). The prominent binding site residues are shown as sticks.]]

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry 1CGT) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-15T13:39:38Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch), its soluble components amylose and amylopectin as well as β-cyclodextrin, a small amylose mimicing cyclic carbohydrate. 

== Structural Features ==

[[File:CBM20_structure_1AC0.png|thumb|300px|right|'''Figure 1.''' The NMR structure of the CBM20 from the Aspergillus niger GH15 glucoamylase with beta-cyclodextrin bound to both binding sites (see [PDB ID 1AC0]). The prominent binding site residues are shown as sticks.]]

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization
:The first structure of CBM20 was the structure of a [[GH13]] CGTase from Bacillus circulans (PDB entry 1CGT) <cite>Klein1991</cite>. The first CBM20 structure with a ligand bound was the


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519

#Klein1991 pmid=1826034
</biblio>
[[Category:Carbohydrate Binding Module Families|CBM020]]

File:CBM20 structure 1AC0.png

2019-11-15T13:36:50Z

Marie Sofie Moeller:

Carbohydrate Binding Module Family 20

2019-11-07T13:38:43Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch) its soluble components amylose and amylopectin as well as β-cyclodextrin, a small amylose mimicing cyclic carbohydrate. 

== Structural Features ==

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is in some cases found associated with enzymes from other CAZy families [[GH31]], [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-07T13:25:25Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch) its soluble components amylose and amylopectin as well as β-cyclodextrin, a small amylose mimicing cyclic carbohydrate. 

== Structural Features ==

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. A CBM20 from an auxiliary activities family [[AA13]] starch polysaccharide monooxygenase was shown to be important for amylose binding and activity on amylose <cite>Vu2019</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is found associated with enzymes from other CAZy families [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582

#Vu2019 pmid=31235519
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-07T11:55:42Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==
CBM20 binds starch granules (raw starch) as well as β-cyclodextrin, a small starch analogue. 

== Structural Features ==

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' The CBM20 from the Aspergillus niger glucoamylase has been shown not only to bind starch but also disrupting its surface, thereby enhancing the amylolytic rate <cite>Southhall1999</cite>. 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is found associated with enzymes from other CAZy families [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560
#Southhall1999 pmid=10218582
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-07T11:37:43Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==


== Structural Features ==

* '''Fold:''' Beta sandwich.
* '''Type:''' Type B 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is found associated with enzymes from other CAZy families [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560

</biblio>

[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-07T11:33:47Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==


== Structural Features ==

* '''Fold:''' Beta sandwich.
* '''Type:''' 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s <cite>Janecek2019</cite>. This is not the case, however, for aromatic residues stacked against glucose rings in binding site 2, which may function to guide the starch chains to the active site and is thus more extended and flexible, undergoing a larger conformational rearrangement when binding the β-cyclodextrin <cite>Sorimachi1997</cite>. While there are two tyrosines (Tyr527 and Tyr556) in the glucoamylase binding site 2, only one aromatic residue (Tyr633, corresponding to the Tyr556) is believed to play the analogous role in the CGTase. On the other hand, a third well-conserved tryptophan residue (Trp563 in glucoamylase and Trp636 in CGTase), although buried and thus not able to interact with β-cyclodextrin directly, was found to be involved in making contacts with several residues at binding site 2 <cite>Sorimachi1997</cite>. 

== Functionalities ==

* '''Functional role of CBM:''' 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is found associated with enzymes from other CAZy families [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560

</biblio>

[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-06T14:39:26Z

Marie Sofie Moeller:

{{UnderConstruction}}
* [[Author]]: ^^^Marie Sofie Møller^^^
* [[Responsible Curator]]s: ^^^Birte Svensson^^^ and ^^^Stephan Janecek^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM20.html
|}
</div>


== Ligand specificities ==


== Structural Features ==

* '''Fold:''' Beta sandwich.
* '''Type:''' 
* '''Features of ligand binding:''' At least one but more typically two binding sites have been found in modules having the CBM20 complexed with bound carbohydrate. Such complexes have been studied for modules originating from several amylolytic enzymes, e.g. GH13_2 CGTase from Bacillus circulans <cite>Penninga1996</cite>, GH14 β-amylase from Bacillus cereus <cite>Mikami1999</cite> and GH15 glucoamylase from Aspergillus niger <cite>Sorimachi1997</cite>, as well as the human glucan phosphatase laforin <cite>Raththagala2015</cite>. The two binding sites of CBM20 have been best illustrated in the NMR structure of the isolated module from A. niger glucoamylase complexed with β-cyclodextrin <cite>Sorimachi1997</cite> and the X-ray structure of the module of the intact B. circulans CGTase in complex with maltose <cite>Penninga1996</cite>. Binding site 1, important for raw starch binding ability, is formed from two tryptophan residues (Trp543 and Trp590 in the glucoamylase and Trp616 and Trp662 in the CGTase) making a compact and rigid hydrophobic site exposed on the surface and well adapted to bind glucose residues in the cyclodextrin ligands, considered as starch mimics. This small and easily accessible site may function as the place where the starch is initially recognized and it in fact does not change conformation after β-cyclodextrin binding compared to the free CBM20 <cite>Sorimachi1996</cite>. It is worth mentioning that both tryptophan residues make stacking interactions with glucose rings and are conserved in the sequence alignment of CBM20s. 

== Functionalities ==

* '''Functional role of CBM:''' 
* '''Most Common Associated Modules:''' The enzymes, of which the CBM20 module constitutes a domain, have predominantly specificities from the ɑ-amylase family [[GH13]] or enzymes from families [[GH70]] and [[GH77]], but can also belong to families [[GH14]] β-amylases and [[GH15]] glucoamylases <cite>Janecek2011</cite>. Among other CAZy GH families, the CBM20 is found associated with enzymes from other CAZy families [[GH57]], [[GH119]] and the auxiliary activities family [[AA13]]. Furthermore, CBM20 modules have been recognised in enzymes of which the catalytic domain is not classified in CAZy. Examples are phosphoglucan, water dikinase, glycerophosphodiester phosphodiesterase-5, laforin, and genethonin-1 <cite>Janecek2019</cite>. The modules of family CBM20 have commonly been found in a single copy and usually appear without SBDs from other CBM families within the same protein, although co-occurence has been observed with [[CBM25]], [[CBM34]], and [[CBM48]] <cite>Janecek2019</cite>.
* '''Novel Applications:''' 

== Family Firsts ==
;First Identified
:The first CBM20 was recognised in the early 1980s at the C-termini of glucoamylases from Aspergillus awamori <cite>Hayashida1982</cite> and Aspergillus niger <cite>Svensson1982 Svensson1983 Boel1984</cite>.
;First Structural Characterization


== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
#Shoseyov2006 pmid=16760304
#Guillen2010 pmid=19908036

#Hayashida1982 Hayashida, S., Kunisaki, S., Nakao, M. and Flor, P.Q. (1982) Evidence for raw starch-affinity site on ''Aspergillus awamori'' glucoamylase I. Agric. Biol. Chem., vol. 46, pp. 83-89.

#Svensson1982 Svensson, B., Pedersen, T.G., Svendsen, I., Sakai, T. and Ottesen, M. (1982) Characterization of two forms of glucoamylase from Aspergillus niger. Carlsb. Res. Commun. vol. 47, pp. 55-69.

#Svensson1983 Svensson, B., Larsen, K., Svendsen, I., and Boel, E. (1983) The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger. Carlsb. Res. Commun. vol. 48, pp. 529-544.

#Boel1984 pmid=6203744
#Janecek2011 pmid=22112614
#Janecek2019 pmid=31536775

#Penninga1996 pmid=8955113
#Mikami1999 pmid=10353816

#Sorimachi1996 pmid=8683599

#Sorimachi1997 pmid=9195884
#Raththagala2015 pmid=25544560

</biblio>

[[Category:Carbohydrate Binding Module Families|CBM020]]

Carbohydrate Binding Module Family 20

2019-11-06T14:19:41Z

Marie Sofie Moeller:

Carbohydrate Binding Module Family 20

2019-11-06T14:18:59Z

Marie Sofie Moeller:

Carbohydrate Binding Module Family 20

2019-11-06T14:12:17Z

Marie Sofie Moeller:

Carbohydrate Binding Module Family 20

2019-11-06T13:29:27Z

Marie Sofie Moeller:

User:Marie Sofie Moeller

2019-11-06T12:18:34Z

Marie Sofie Moeller:

[[Image:Press_photo_MarieSMoeller.jpg|200px|right]]
<div>
In 2013 Marie Sofie Møller completed her PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem at the Technical University of Denmark. She has mainly been focusing on structure-function relationship studies of glycoside hydrolases from family [[GH13]]. At the Carlsberg Research Laboratory under supervision by Anette Henriksen, she has been determining several structures of GH13_13 barley limit dextrinase including the first structure of an ɑ-glucan debranching enzyme in complex with a natural substrate, i.e. a branched maltooligosaccharide (limit dextrin). Furthermore, she has determined the complex structure between barley limit dextrinase and its endogenous inhibitor, a 13.4 kDa cereal type inhibitor. The study of the latter complex resulted in a spin-off project, which she got granted by an individual postdoc grant from the Independent Research Fund Denmark. The project was carried out in the laboratory of Ingemar André at Lund University, Sweden. The spin-off project focused on understanding the high-affinity (pM) using computational redesign.

In 2016 she returned to the Technical University of Denmark, where she holds a position as Assistant Professor in the group of ^^^Birte Svensson^^^. She is currently working on a project on low affinity protein-carbohydrate interactions focusing on carbohydrate binding module families [[CBM10]] and [[CBM45]]. The CBM10s studied originate from a [[GH5]] subfamily 8 mannanase from a marine bacterium, while the CBM45s originate from a glucan, water dikinase from potato.

----

<biblio>
#Jensen2011 pmid=21539920
#Moeller2012a pmid=22949184
#Moeller2012b pmid=22685275
#Moeller2015a pmid=25562209
#Moeller2015b pmid=25792743
#Moeller2016a pmid=27137180
#Moeller2016b pmid=27450115
#Moeller2017 pmid=28411221
#Wilkens2018 pmid=30483298
#Holck2019 pmid=31558605

#Andersen2019 pmid=31676454
</biblio>


[[Category:Contributors|Moeller,Marie-Sofie]]

User:Marie Sofie Moeller

2019-11-06T12:02:26Z

Marie Sofie Moeller:

[[Image:Press_photo_MarieSMoeller.jpg|200px|right]]
<div>
In 2013 Marie Sofie Møller completed her PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem at the Technical University of Denmark. She has mainly been focusing on structure-function relationship studies of glycoside hydrolases from family [[GH13]] <cite>Moeller2012a Moeller2012b</cite>. At the Carlsberg Research Laboratory under supervision by Anette Henriksen, she has been determining several structures of GH13_13 barley limit dextrinase including the first structure of an a-glucan debranching enzyme in complex with a natural substrate, i.e. a branched maltooligosaccharide (limit dextrin). Furthermore, she has determined the complex structure between barley limit dextrinase and its endogenous inhibitor, a 13.4 kDa cereal type inhibitor. The study of the latter complex resulted in a spin-off project, which she got granted by an individual postdoc grant from the Independent Research Fund Denmark. The project was carried out in the laboratory of Ingemar André at Lund University, Sweden. The spin-off project focused on understanding the high-affinity (pM) using computational redesign.
In 2016 she returned to the Technical University of Denmark, where she holds a position as Assistant Professor in the group of ^^^Birte Svensson^^^. She is currently working on a project on low affinity protein-carbohydrate interactions focusing on carbohydrate binding module families [[CBM10]] and [[CBM45]]. The CBM10s studied originate from a [[GH5]] subfamily 8 mannanase from a marine bacterium, while the CBM45s originate from a glucan, water dikinase from potato.

----

<biblio>
#Moeller2012a pmid=22949184

#Moeller2012b pmid=22685275

</biblio>


[[Category:Contributors|Moeller,Marie-Sofie]]

File:Press photo MarieSMoeller.jpg

2019-11-06T11:45:50Z

Marie Sofie Moeller: