Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D (CenD), a family A beta-1,4-glucanase

Author:

Meinke A1,Gilkes N R1,Kilburn D G1,Miller R C1,Warren R A1

Affiliation:

1. Department of Microbiology, University of British Columbia, Vancouver, Canada.

Abstract

Five cellulose-binding polypeptides were detected in Cellulomonas fimi culture supernatants. Two of them are CenA and CenB, endo-beta-1,4-glucanases which have been characterized previously; the other three were previously uncharacterized polypeptides with apparent molecular masses of 120, 95, and 75 kDa. The 75-kDa cellulose-binding protein was designated endoglucanase D (CenD). The cenD gene was cloned and sequenced. It encodes a polypeptide of 747 amino acids. Mature CenD is 708 amino acids long and has a predicted molecular mass of 74,982 Da. Analysis of the predicted amino acid sequence of CenD shows that the enzyme comprises four domains which are separated by short linker polypeptides: an N-terminal catalytic domain of 405 amino acids, two repeated sequences of 95 amino acids each, and a C-terminal domain of 105 amino acids which is > 50% identical to the sequences of cellulose-binding domains in Cex, CenA, and CenB from C. fimi. Amino acid sequence comparison placed the catalytic domain of CenD in family A, subtype 1, of beta-1,4-glycanases. The repeated sequences are more than 40% identical to the sequences of three repeats in CenB and are related to the repeats of fibronectin type III. CenD hydrolyzed the beta-1,4-glucosidic bond with retention of anomeric configuration. The activities of CenD towards various cellulosic substrates were quite different from those of CenA and CenB.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference42 articles.

1. Al-Tawheed A. R. 1988. M.Sc. thesis Trinity College Dublin Ireland.

2. The Glu residue in the conserved Asn-Glu-Pro sequence of two highly divergent endo-,- 1,4-glucanases is essential for enzymatic activity;Baird S. D.;Biochem. Biophys. Res. Commun.,1990

3. Stereochemistry of hydrolysis catalysed by endoglucanase Z from Erwinia chrysanthemi;Barras F.;FEBS Lett.,1992

4. Molecular biology of cellulose degradation. Annu;Beguin P.;Rev. Microbiol.,1990

5. Cloning of cellulase genes;Biguin P.;Crit. Rev. Biotechnol.,1987

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3