Rational Engineering of Mannosyl Binding in the Distal Glycone Subsites of Cellulomonas fimi Endo-β-1,4-mannanase: Mannosyl Binding Promoted at Subsite −2 and Demoted at Subsite −3,-Reference-Cited by-同舟云学术

Rational Engineering of Mannosyl Binding in the Distal Glycone Subsites of Cellulomonas fimi Endo-β-1,4-mannanase: Mannosyl Binding Promoted at Subsite −2 and Demoted at Subsite −3,

Published:2010-05-20 Issue:23 Volume:49 Page:4884-4896
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hekmat Omid¹,Lo Leggio Leila²,Rosengren Anna¹,Kamarauskaite Jurate²³,Kolenova Katarina¹,Stålbrand Henrik¹

Affiliation:

1. Department of Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, Box 124, SE-221 00 Lund, Sweden

2. Biophysical Chemistry Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark

3. Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi100097f

Reference59 articles.

1. Isolation and characterization of galactoglucomannan from spruce ( Picea abies )

2. How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation

3. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

4. β-Glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes wit 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven

5. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.

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