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Difference between revisions of "Carbohydrate Binding Module Family 82"

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* [[Author]]: ^^^Darrell Cockburn^^^
 
* [[Responsible Curator]]:  ^^^Nicole Koropatkin^^^
 
* [[Responsible Curator]]:  ^^^Nicole Koropatkin^^^
 
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== Ligand specificities ==
 
== Ligand specificities ==
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.
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[[File:Amy13K_CBM82_highlight.jpg|thumb|600px|right|'''Figure 1. Domain architecture of ''E. rectale'' Amy13K''' The CBM and GH families are noted. The 'S' indicate the signal sequence and the 'anchor' is a cell wall anchor region. The unknown domain has no known function, however, deletion eliminates enzyme activity <cite>Cockburn2018</cite>.]]
  
''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010 Armenta2017</cite>.
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The founding member of this family and the first module to be characterized is the first CBM found in the cell-wall anchored [[GH13]] enzyme Amy13K from ''Eubacterium rectale'' (see Fig1). It was found to bind beta-cyclodextrin and glycogen with similar affinity, with slightly weaker affinity for maltoheptaose as determined by isothermal titration calorimetry. The module was also found to bind to corn starch granules, both from a wild-type source and from a high amylose source (HiMaize 260) with approximately equal affinity but did not demonstrate binding to potato starch or a chemically crosslinked starch (Fibersym) as determined via depletion assays. Binding to amylopectin and pullulan was also demonstrated via affinity electrophoresis.
 +
<cite>Cockburn2018</cite>.
  
 
== Structural Features ==
 
== Structural Features ==
''Content in this section should include, in paragraph form, a description of:''
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Secondary structure analysis and alignments suggest they are likely to be beta-sandwich type folds similar to the [[CBM41]] family <cite>Cockburn2018</cite>.  
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)
 
* '''Type:''' Include here Type A, B, or C and properties
 
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.
 
  
 
== Functionalities ==  
 
== Functionalities ==  
''Content in this section should include, in paragraph form, a description of:''
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This family has been found to be exclusively associated with [[GH13]] family amylases from a quite narrow taxonomic range within ''Roseburia'' and ''Eubacterium rectale'' <cite>Cockburn2018</cite>. Removal of the only CBM82 from the ''E. rectale'' Amy13K enzyme resulted in an approximately 2-fold decrease in activity of the enzyme towards amylopectin or potato starch, but resulted in a larger 5-fold decrease in the activity of the enzyme towards corn starch granules, suggesting an important role in targeting the enzyme to this substrate. <cite>Cockburn2018</cite> 
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
 
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
 
* '''Novel Applications:'''  Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.
 
  
 
== Family Firsts ==
 
== Family Firsts ==
;First Identified
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;First Identified: In ''Roseburia inulinivorans'' as a predicted CBM <cite>Ramsay2006</cite>
:Insert archetype here, possibly including ''very brief'' synopsis.
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;First Structural Characterization
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;First Characterized: From ''E. rectale'' Amy13K, establishing the family <cite>Cockburn2018</cite>
:Insert archetype here, possibly including ''very brief'' synopsis.
 
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
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#Cockburn2018 pmid=29139580
#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].
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#Ramsay2006 pmid=17074899
#Boraston2004 pmid=15214846
 
#Hashimoto2006 pmid=17131061
 
#Shoseyov2006 pmid=16760304
 
#Guillen2010 pmid=19908036
 
#Armenta2017 pmid=28547780
 
 
</biblio>
 
</biblio>
  
 
[[Category:Carbohydrate Binding Module Families|CBM082]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. -->
 
[[Category:Carbohydrate Binding Module Families|CBM082]] <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. -->

Revision as of 23:15, 13 May 2019

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This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.


CAZy DB link
http://www.cazy.org/CBM82.html

Ligand specificities

Figure 1. Domain architecture of E. rectale Amy13K The CBM and GH families are noted. The 'S' indicate the signal sequence and the 'anchor' is a cell wall anchor region. The unknown domain has no known function, however, deletion eliminates enzyme activity [1].

The founding member of this family and the first module to be characterized is the first CBM found in the cell-wall anchored GH13 enzyme Amy13K from Eubacterium rectale (see Fig1). It was found to bind beta-cyclodextrin and glycogen with similar affinity, with slightly weaker affinity for maltoheptaose as determined by isothermal titration calorimetry. The module was also found to bind to corn starch granules, both from a wild-type source and from a high amylose source (HiMaize 260) with approximately equal affinity but did not demonstrate binding to potato starch or a chemically crosslinked starch (Fibersym) as determined via depletion assays. Binding to amylopectin and pullulan was also demonstrated via affinity electrophoresis. [1].

Structural Features

Secondary structure analysis and alignments suggest they are likely to be beta-sandwich type folds similar to the CBM41 family [1].

Functionalities

This family has been found to be exclusively associated with GH13 family amylases from a quite narrow taxonomic range within Roseburia and Eubacterium rectale [1]. Removal of the only CBM82 from the E. rectale Amy13K enzyme resulted in an approximately 2-fold decrease in activity of the enzyme towards amylopectin or potato starch, but resulted in a larger 5-fold decrease in the activity of the enzyme towards corn starch granules, suggesting an important role in targeting the enzyme to this substrate. [1]

Family Firsts

First Identified
In Roseburia inulinivorans as a predicted CBM [2]
First Characterized
From E. rectale Amy13K, establishing the family [1]

References

  1. Cockburn DW, Suh C, Medina KP, Duvall RM, Wawrzak Z, Henrissat B, and Koropatkin NM. (2018). Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut. Mol Microbiol. 2018;107(2):249-264. DOI:10.1111/mmi.13881 | PubMed ID:29139580 [Cockburn2018]
  2. Ramsay AG, Scott KP, Martin JC, Rincon MT, and Flint HJ. (2006). Cell-associated alpha-amylases of butyrate-producing Firmicute bacteria from the human colon. Microbiology (Reading). 2006;152(Pt 11):3281-3290. DOI:10.1099/mic.0.29233-0 | PubMed ID:17074899 [Ramsay2006]

All Medline abstracts: PubMed