STEREOCHEMICAL COURSE OF THE HYDROLYSIS REACTION CATALYZED BY CHITINASE-A1 AND CHITINASE-D FROM BACILLUS-CIRCULANS WL-12

被引：69

作者：

ARMAND, S

TOMITA, H

HEYRAUD, A

GEY, C

WATANABE, T

HENRISSAT, B

机构：

[1] UNIV GRENOBLE 1, CTR RECH MACROMOLEC VEGETALES, CNRS, F-38041 GRENOBLE, FRANCE

[2] NIIGATA UNIV, FAC AGR, DEPT APPL BIOL CHEM, NIIGATA 95021, JAPAN

来源：

FEBS LETTERS | 1994年 / 343卷 / 02期

关键词：

CHITINASE; REACTION MECHANISM; HYDROLYSIS; CHITOOLIGOSACCHARIDE; BACILLUS CIRCULANS WL-12;

D O I：

10.1016/0014-5793(94)80314-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Chitinases Al 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. H-1 NMR spectroscopy of the hydrolysis of chitotetraitol showed that this anomer corresponds to beta-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.

引用

页码：177 / 180

页数：4

共 19 条

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