EC 3.2.1.14 - Chitinase

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IntEnz Enzyme Nomenclature
EC 3.2.1.14

Names

Accepted name:
chitinase
Other names:
1,4-β-poly-N-acetylglucosaminidase
β-1,4-poly-N-acetyl glucosamidinase
chitodextrinase [ambiguous]
poly-β-glucosaminidase
poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase
ChiC
Systematic name:
(1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase

Reaction

Comments:

The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00620 , PROSITE:PDOC00839
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004568
CAS Registry Number: 9001-06-3
UniProtKB/Swiss-Prot: (172) [show] [UniProt]

References

  1. Fischer, E.H. and Stein, E.A.
    Cleavage of O- and S-glycosidic bonds (survey).
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 4, Academic Press, New York, 1960, 301-312
  2. Tracey, M.V.
    Chitinase in some basidiomycetes.
    Biochem. J. 61: 579-586 (1955). [PMID: 13276340]
  3. Zechmeister, L. and Tóth, G.
    Chromatographic adsorption of the enzymes of emulsin which act on chitins.
    Enzymologia 7: 165-169 (1939).
  4. Connell, T. D., Metzger, D. J., Lynch, J., Folster, J. P.
    Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae.
    J. Bacteriol. 180: 5591-5600 (1998). [PMID: 9791107]
  5. Francetic, O., Badaut, C., Rimsky, S., Pugsley, A. P.
    The ChiA (YheB) protein of Escherichia coli K-12 is an endochitinase whose gene is negatively controlled by the nucleoid-structuring protein H-NS.
    Mol. Microbiol. 35: 1506-1517 (2000). [PMID: 10760150]
  6. Zverlov, V. V., Fuchs, K. P., Schwarz, W. H.
    Chi18A, the endochitinase in the cellulosome of the thermophilic, cellulolytic bacterium Clostridium thermocellum.
    Appl. Environ. Microbiol. 68: 3176-3179 (2002). [PMID: 12039789]
  7. Rottloff, S., Stieber, R., Maischak, H., Turini, F. G., Heubl, G., Mithöfer, A.
    Functional characterization of a class III acid endochitinase from the traps of the carnivorous pitcher plant genus, Nepenthes.
    J. Exp. Bot. 62: 4639-4647 (2011). [PMID: 21633084]

[EC 3.2.1.14 created 1961, modified 2017]