Stereochemical course of the hydrolysis reaction catalyzed by chitinases Al and D from Bacillus circulans WL‐12

FEBS Letters

Henrissat, B.¹  Watanabe, T.²  Heyraud, A.¹  Gey, C.¹  Armand, S.¹  Tomita, H.² 

[1] Centre de Recherches sur les Macromolécules Végétales1, CNRS, P 53X, F-38041 Grenoble, France;Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, 8050 Ikarashi-2, Niigata 950-21, Japan

关键词: Chitinase;    Reaction mechanism;    Hydrolysis;    Chitooligosaccharide;    Bacillus circulans WL-12;   

DOI  :  10.1016/0014-5793(94)80314-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 β-chitobiose, demonstrating that chitinases Al 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.

【 授权许可】

Unknown