THE BETA-MANNANASE FROM CALDOCELLUM-SACCHAROLYTICUM IS PART OF A MULTIDOMAIN ENZYME

被引：72

作者：

GIBBS, MD ^{[1
]}

SAUL, DJ ^{[1
]}

LUTHI, E ^{[1
]}

BERGQUIST, PL ^{[1
]}

机构：

[1] UNIV AUCKLAND, DEPT CELLULAR & MOLEC BIOL, CTR GENE TECHNOL, AUCKLAND, NEW ZEALAND

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 1992年 / 58卷 / 12期

关键词：

D O I：

10.1128/AEM.58.12.3864-3867.1992

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The complete sequence of a beta-mannanase gene from an anaerobic extreme thermophile was determined, and it shows that the expressed protein consists of two catalytic domains and two binding domains separated by spacer regions rich in proline and threonine residues. The amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase. Neither domain shows homology with any other cellulase or hemicellulase sequence at the nucleic acid or protein level.

引用

页码：3864 / 3867

页数：4

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