The NodB domain of a multidomain xylanase from Cellulomonas fimi deacetylates acetylxylan

被引：37

作者：

Laurie, JI

Clarke, JH

Ciruela, A

Faulds, CB

Williamson, G

Gilbert, HJ

Rixon, JE

MillwardSadler, J

Hazlewood, GP

机构：

[1] BABRAHAM INST, DEPT CELLULAR PHYSIOL, CAMBRIDGE CB2 4AT, ENGLAND

[2] INST FOOD RES, DEPT BIOCHEM, NORWICH NR4 7UA, NORFOLK, ENGLAND

[3] UNIV NEWCASTLE UPON TYNE, FAC AGR & BIOL SCI, DEPT BIOL & NUTR SCI, NEWCASTLE UPON TYNE NE1 7RU, TYNE & WEAR, ENGLAND

来源：

FEMS MICROBIOLOGY LETTERS | 1997年 / 148卷 / 02期

基金：

英国生物技术与生命科学研究理事会;

关键词：

Cellulomonas fimi; xylanase structure; NodB domain; deacetylase;

D O I：

10.1016/S0378-1097(97)00046-3

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The NodB-like domain from Cellulomonas fimi xylanase D is a member of a small family of structurally homologous proteins which includes a chitin deacetylase from Mucor r ouxlr, an acetylxylan esterase from Stleptomyces livirlans and the NodB protein from rhizobia. Functional analysis of the xylanase D NodB domain suggests that, like other members of the family, it is a deacetylase, whose function is to remove acetyl groups from acetylated xylan.

引用

页码：261 / 264

页数：4

共 18 条

[1] Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates [J].