title: Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12.
abstract: Chitinases A1 and D were purified from the periplasmic proteins produced by Escherichia coli HB101 harbouring recombinant plasmids carrying respectively the chiA and chiD genes of Bacillus circulans WL-12. HPLC analysis indicated that during the hydrolysis of chitotriose, both chitinases initially produce N-acetylglucosamine and only one anomer of chitobiose. 1H NMR spectroscopy of the hydrolysis of chitotetraitol showed that this anomer corresponds to beta-chitobiose, demonstrating that chitinases A1 and D act by a molecular mechanism that retains the anomeric configuration. This mechanism is similar to that of lysozymes although both chitinases belong to a family of proteins sharing no demonstrable amino acid sequence similarity with lysozymes.
authors.affiliation: Centre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble, France.
authors.forename: S
authors.initials: S
authors.lastname: Armand
authors.forename: H
authors.initials: H
authors.lastname: Tomita
authors.forename: A
authors.initials: A
authors.lastname: Heyraud
authors.forename: C
authors.initials: C
authors.lastname: Gey
authors.forename: T
authors.initials: T
authors.lastname: Watanabe
authors.forename: B
authors.initials: B
authors.lastname: Henrissat
mesh_terms: D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D002384:Catalysis; D002688:Chitinases / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D002688:Chitinases