CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 46

2010-02-16T17:22:37Z

Marie-Eve Lacombe-Harvey:

{{CuratorApproved}}
* [[Author]]: ^^^Ryszard Brzezinski^^^
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH46'''
|-
|'''Clan'''
|GH-I
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH46.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 46 are essentially all ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity acted upon the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.

== Kinetics and Mechanism ==
Family GH46 enzymes utilize an [[inverting]] mechanism, as shown by NMR <cite>Fukamizo1995</cite>.

== Catalytic Residues ==
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The [[general acid]] residue is Glu22 in the sequence SSA'''E'''NSS, while Asp40 (DIG'''D'''GRG) is the [[general base]] residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY'''T'''GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''E'''QDD) , Asp55 (DIE'''D'''ERG) and Thr60 (RGY'''T'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.

== Three-dimensional structures ==
[[File:csn_entire_5a.png|200px|thumb|right|3D structure of the chitosanase from ''Streptomyces'' sp. N174]]
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>.
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>.

== Family Firsts ==
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.
;First [[general base]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First [[general acid]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.

== References ==
<biblio>
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.
#Fukamizo1995 pmid=7487871
#Boucher1995 pmid=8537367
#Lacombe-Harvey2009 pmid=19143844
#Saito1999 pmid=10521473
#Marcotte1996 pmid=8564542
#Fukamizo2005 pmid=16272568
#Monzingo1996 pmid=8564539
#Holm1994 pmid=8119396
#Tremblay2001 pmid=11686931
#Katsumi2005 pmid=16288718
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.
</biblio>

[[Category:Glycoside Hydrolase Families|GH046]]

File:Csn entire 5a.png

2010-02-16T17:18:36Z

Marie-Eve Lacombe-Harvey:

File:Csn entire 5.png

2010-02-16T17:17:05Z

Marie-Eve Lacombe-Harvey: uploaded a new version of "File:Csn entire 5.png"

Csn N174

Glycoside Hydrolase Family 46

2010-02-16T16:52:33Z

Marie-Eve Lacombe-Harvey:

{{CuratorApproved}}
* [[Author]]: ^^^Ryszard Brzezinski^^^
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH46'''
|-
|'''Clan'''
|GH-I
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH46.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 46 are essentially all ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity acted upon the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.

== Kinetics and Mechanism ==
Family GH46 enzymes utilize an [[inverting]] mechanism, as shown by NMR <cite>Fukamizo1995</cite>.

== Catalytic Residues ==
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The [[general acid]] residue is Glu22 in the sequence SSA'''E'''NSS, while Asp40 (DIG'''D'''GRG) is the [[general base]] residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY'''T'''GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''E'''QDD) , Asp55 (DIE'''D'''ERG) and Thr60 (RGY'''T'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.

== Three-dimensional structures ==
[[File:csn_entire_5.png|200px|thumb|right|3D structure]]
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>.
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>.

== Family Firsts ==
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.
;First [[general base]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First [[general acid]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.

== References ==
<biblio>
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.
#Fukamizo1995 pmid=7487871
#Boucher1995 pmid=8537367
#Lacombe-Harvey2009 pmid=19143844
#Saito1999 pmid=10521473
#Marcotte1996 pmid=8564542
#Fukamizo2005 pmid=16272568
#Monzingo1996 pmid=8564539
#Holm1994 pmid=8119396
#Tremblay2001 pmid=11686931
#Katsumi2005 pmid=16288718
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.
</biblio>

[[Category:Glycoside Hydrolase Families|GH046]]

Glycoside Hydrolase Family 46

2010-02-16T16:51:48Z

Marie-Eve Lacombe-Harvey:

{{CuratorApproved}}
* [[Author]]: ^^^Ryszard Brzezinski^^^
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH46'''
|-
|'''Clan'''
|GH-I
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH46.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 46 are essentially all ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity acted upon the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.

== Kinetics and Mechanism ==
Family GH46 enzymes utilize an [[inverting]] mechanism, as shown by NMR <cite>Fukamizo1995</cite>.

== Catalytic Residues ==
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The [[general acid]] residue is Glu22 in the sequence SSA'''E'''NSS, while Asp40 (DIG'''D'''GRG) is the [[general base]] residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY'''T'''GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''E'''QDD) , Asp55 (DIE'''D'''ERG) and Thr60 (RGY'''T'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.

== Three-dimensional structures ==
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>.
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>.
[[File:csn_entire_5.png|200px|thumb|right|3D structure]]
== Family Firsts ==
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.
;First [[general base]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First [[general acid]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.

== References ==
<biblio>
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.
#Fukamizo1995 pmid=7487871
#Boucher1995 pmid=8537367
#Lacombe-Harvey2009 pmid=19143844
#Saito1999 pmid=10521473
#Marcotte1996 pmid=8564542
#Fukamizo2005 pmid=16272568
#Monzingo1996 pmid=8564539
#Holm1994 pmid=8119396
#Tremblay2001 pmid=11686931
#Katsumi2005 pmid=16288718
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.
</biblio>

[[Category:Glycoside Hydrolase Families|GH046]]

Glycoside Hydrolase Family 46

2010-02-16T16:50:08Z

Marie-Eve Lacombe-Harvey:

{{CuratorApproved}}
* [[Author]]: ^^^Ryszard Brzezinski^^^
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH46'''
|-
|'''Clan'''
|GH-I
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/fam/GH46.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of family 46 are essentially all ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity acted upon the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.

== Kinetics and Mechanism ==
Family GH46 enzymes utilize an [[inverting]] mechanism, as shown by NMR <cite>Fukamizo1995</cite>.

== Catalytic Residues ==
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The [[general acid]] residue is Glu22 in the sequence SSA'''E'''NSS, while Asp40 (DIG'''D'''GRG) is the [[general base]] residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY'''T'''GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''E'''QDD) , Asp55 (DIE'''D'''ERG) and Thr60 (RGY'''T'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.

== Three-dimensional structures ==
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>.
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>.
[[File:csn_entire_5.png|200px|thumb|left|alt text]]
== Family Firsts ==
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.
;First [[general base]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First [[general acid]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.

== References ==
<biblio>
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.
#Fukamizo1995 pmid=7487871
#Boucher1995 pmid=8537367
#Lacombe-Harvey2009 pmid=19143844
#Saito1999 pmid=10521473
#Marcotte1996 pmid=8564542
#Fukamizo2005 pmid=16272568
#Monzingo1996 pmid=8564539
#Holm1994 pmid=8119396
#Tremblay2001 pmid=11686931
#Katsumi2005 pmid=16288718
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.
</biblio>

[[Category:Glycoside Hydrolase Families|GH046]]

File:Csn entire 5.png

2010-02-16T16:43:54Z

Marie-Eve Lacombe-Harvey: Csn N174

Csn N174