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Difference between revisions of "Glycoside Hydrolase Family 80"

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== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
The stereochemistry of the hydrolytic reaction catalyzed by GH80 members has not yet been studied. However, sequence similarity with members of [[Clan]] GH-I suggests that these enzymes may operate with inversion of the anomeric configuration (see [[#Catalytic Residues]], below)
+
The stereochemistry of the hydrolytic reaction catalyzed by GH80 members has not yet been studied. However, sequence similarity with members of [[Clan]] GH-I suggests that these enzymes may operate with inversion of the anomeric configuration (see ''Catalytic Residues'', below)
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.
+
The chitosanases from family GH80 share a PROSITE signature motif <cite>Sigrist2010</cite> with the chitosanases from family [[GH46]] <cite>Tremblay2000</cite>.  Together with [[GH24]], these three families comprise [[Clan]] GH-I <cite>CAZYGHpage</cite>.
  
 
A site-directed mutagenesis study of the chitosanase A from ''Matsuebacter chitosanotabidus'' 3001 (new name: ''Mitsuaria chitosanitabida'' <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
 
A site-directed mutagenesis study of the chitosanase A from ''Matsuebacter chitosanotabidus'' 3001 (new name: ''Mitsuaria chitosanitabida'' <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
 
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
No three-dimensional structure has been solved for this family.
+
No three-dimensional structure has yet been solved for this family.
  
 
== Family Firsts ==
 
== Family Firsts ==
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#Sigrist2010 pmid=19858104
 
#Sigrist2010 pmid=19858104
 
#Amakata2005 pmid=16166689
 
#Amakata2005 pmid=16166689
 
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#CAZYGHpage http://www.cazy.org/Glycoside-Hydrolases.html
 
 
 
 
 
 
 
 
  
 
[[Category:Glycoside Hydrolase Families|GH080]]
 
[[Category:Glycoside Hydrolase Families|GH080]]

Revision as of 06:05, 18 July 2011

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Glycoside Hydrolase Family GH80
Clan GH-I
Mechanism not determined
Active site residues inferred
CAZy DB link
http://www.cazy.org/GH80.html


Substrate specificities

Glycoside hydrolase family GH80 is comprised of endo-acting beta-1,4-chitosanases of bacterial origin. The first characterized member was from a proteobacterium [1] belonging to the Bacteroidetes/Chlorobi group [2, 3]. At present (July 2011), GH80 is very small family, comprised of fewer than 20 members.

Characterized GH80 members do not hydrolyze chitin or cellulose [1, 3], and for one member, the chitosan hexa-oligosaccharide (GlcN)6 is preferentially hydrolyzed into two molecules of the trisaccharide [4].

Kinetics and Mechanism

The stereochemistry of the hydrolytic reaction catalyzed by GH80 members has not yet been studied. However, sequence similarity with members of Clan GH-I suggests that these enzymes may operate with inversion of the anomeric configuration (see Catalytic Residues, below)

Catalytic Residues

The chitosanases from family GH80 share a PROSITE signature motif [5] with the chitosanases from family GH46 [6]. Together with GH24, these three families comprise Clan GH-I [7].

A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida [8]) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YPENG)and Glu-141 (in the sequence DYEAA) [4].

Three-dimensional structures

No three-dimensional structure has yet been solved for this family.

Family Firsts

First primary sequence determination
Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) [1, 8]
First stereochemistry determination
Not yet determined
First catalytic nucleophile identification
Not yet identified
First general acid/base residue identification
Not yet identified
First 3-D structure
Not yet determined

References

<biblio>

  1. Park1999 pmid=10542164
  2. Matsuda2001 Matsuda, Y., Iida, I., Shinogi, T., Kakutani, K., Nonomura, T., Toyoda, H. (2001) In vitro suppression of mycelial growth of Fusarium oxysporum by extracellular chitosanase of Sphingobacterium multivorum and cloning of the chitosanase gene csnSM1. J. Gen. Plant Pathol. 67, 318-324.
  3. Yi2004 Yi, J.-H., Jang, H.-K., Lee, S.-J., Lee, K.-E., Choi, S.-G. (2004) Purification and properties of chitosanase from chitinolytic beta-Proteobacterium KNU3. J. Microbiol. Biotechnol. 14, 337-343.
  4. Shimono2002 pmid=11754739
  5. Tremblay2000 pmid=11068683
  6. Sigrist2010 pmid=19858104
  7. Amakata2005 pmid=16166689
  8. CAZYGHpage http://www.cazy.org/Glycoside-Hydrolases.html