Contribution of Domain Interactions and Calcium Binding to the Stability of Carbohydrate-Active Enzymes-Reference-Cited by-同舟云学术

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Contribution of Domain Interactions and Calcium Binding to the Stability of Carbohydrate-Active Enzymes

Published:2014-04-30 Issue: Volume: Page:115-127
ISSN:
Container-title:Bioenergy
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Author:

Ljungdahl Lars G.¹,Kataeva Irina A.²,Uversky Vladimir N.³

Affiliation:

1. Department of Biochemistry and Molecular Biology, A216 Fred Davison Life Sciences Complex; University of Georgia; Athens GA 30602

2. Department of Biochemistry and Molecular Biology, B222A Fred Davison Life Sciences Complex; University of Georgia; Athens GA 30602

3. Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics; Indiana University School of Medicine; 635 Narnhill Dr. MS 4021 Indianapolis IN 46202-3763

Publisher

ASM Press

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1128/9781555815547.ch9/fullpdf

Reference66 articles.

1. Cloning, DNA sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome;Ahsan;J. Bacteriol,1996

2. Characterization of a cellulose containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis;Arai;J. Bacteriol,2003

3. The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides;Shoham;Annu. Rev. Microbiol,2004

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