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PROSITE documentation PDOC00839

Chitinases family 18 active site





Description

Chitinases (EC 3.2.1.14) [1] are enzymes that catalyze the hydrolysis of the β-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. From the view point of sequence similarity chitinases belong to either family 18 or 19 in the classification of glycosyl hydrolases [2,E1]. Chitinases of family 18 (also known as classes III or V) groups a variety of proteins:

 a) Chitinases from:

 - Prokaryotes such as Alteromonas, Bacillus, Serratia, Streptomyces, etc.
 - Plants such as Arabidopsis, cucumber, bean, tobacco, etc.
 - Fungi such as Aphanocladium, Rhizopus, Saccharomyces, etc.
 - Nematode (Brugia malayi).
 - Insects (Manduca sexta).
 - Baculoviruses (Autographa Californica Nuclear Polyhedrosis virus).

 b) Other proteins:

 - Hevamine, a rubber tree protein with chitinase and lysozyme activities.
 - Kluyveromyces lactis killer toxin alpha subunit, which acts as a chitinase.
 - Flavobacterium and Streptomyces endo-beta-N-acetylglucosaminidases (EC 3.2.
   1.96).
 - Mammalian  di-N-acetylchitobiase  which  is  involved in the degradation of
   asparagine-linked glycoproteins.
 - Human cartilage glycoprotein Gp-39.
 - Jack  bean  concanavalin  B  (conB),  a protein that has lost its catalytic
   activity.

Site directed mutagenesis experiments [3] and crystallographic data [4,5] have shown that a conserved glutamate is involved in the catalytic mechanism and probably acts as a proton donor. This glutamate is at the extremity of the best conserved region in these proteins.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Expert(s) to contact by email:

Neuhaus J.-M.
Henrissat B.

Last update:

November 1997 / Text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CHITINASE_18, PS01095; Chitinases family 18 active site  (PATTERN)


References

1AuthorsFlach J. Pilet P.-E. Jolles P.
TitleWhat's new in chitinase research?
SourceExperientia 48:701-716(1992).
PubMed ID1516675

2AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104

3AuthorsManya H. Aoki J. Watanabe M. Adachi T. Asou H. Inoue Y. Arai H. Inoue K.
TitleSwitching of platelet-activating factor acetylhydrolase catalytic subunits in developing rat brain.
SourceJ. Biol. Chem. 273:18567-18572(1998).
PubMed ID9660828

4AuthorsPerrakis A. Tews I. Dauter Z. Oppenheim A.B. Chet I. Wilson K.S. Vorgias C.E.
TitleCrystal structure of a bacterial chitinase at 2.3 A resolution.
SourceStructure 2:1169-1180(1994).
PubMed ID7704527

5Authorsvan Scheltinga A.C.T. Kalk K.H. Beintema J.J. Dijkstra B.W.
SourceStructure 2:1181-1189(1994).

E1Titlehttps://www.uniprot.org/docs/glycosid



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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