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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.

Neuhaus J.-M.
Henrissat B.

November 1997 / Text revised.

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

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

Consensus pattern: [LIVMFY]-[DN]-G-[LIVMF]-[DN]-[LIVMF]-[DN]-x-E E is the active site residue Sequences known to belong to this class detected by the pattern: ALL, except for conB which has a Gln instead of the active site Glu Other sequence(s) detected in Swiss-Prot: 1.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01095 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01095 • Scan Swiss-Prot/TrEMBL entries against PS01095 • view ligand binding statistics

Matching PDB structures: 1C3F 1CTN 1D2K 1EDT ... [ALL]

1	Authors	Flach J., Pilet P.-E., Jolles P.
	Title	What's new in chitinase research?
	Source	Experientia 48:701-716(1992).
	PubMed ID	1516675

2	Authors	Henrissat B.
	Title	A classification of glycosyl hydrolases based on amino acid sequence similarities.
	Source	Biochem. J. 280:309-316(1991).
	PubMed ID	1747104

3	Authors	Manya H., Aoki J., Watanabe M., Adachi T., Asou H., Inoue Y., Arai H., Inoue K.
	Title	Switching of platelet-activating factor acetylhydrolase catalytic subunits in developing rat brain.
	Source	J. Biol. Chem. 273:18567-18572(1998).
	PubMed ID	9660828

4	Authors	Perrakis A., Tews I., Dauter Z., Oppenheim A.B., Chet I., Wilson K.S., Vorgias C.E.
	Title	Crystal structure of a bacterial chitinase at 2.3 A resolution.
	Source	Structure 2:1169-1180(1994).
	PubMed ID	7704527

5	Authors	van Scheltinga A.C.T., Kalk K.H., Beintema J.J., Dijkstra B.W.
	Source	Structure 2:1181-1189(1994).

E1
Source	http://www.uniprot.org/docs/glycosid

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