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Title: Novel {alpha}-glucosidase from human gut microbiome : substrate specificities and their switch.

Abstract

The human intestine harbors a large number of microbes forming a complex microbial community that greatly affects the physiology and pathology of the host. In the human gut microbiome, the enrichment in certain protein gene families appears to be widespread. They include enzymes involved in carbohydrate metabolism such as glucoside hydrolases of dietary polysaccharides and glycoconjugates. We report the crystal structures (wild type, 2 mutants, and a mutant/substrate complex) and the enzymatic activity of a recombinant {alpha}-glucosidase from human gut bacterium Ruminococcus obeum. The first ever protein structures from this bacterium reveal a structural homologue to human intestinal maltase-glucoamylase with a highly conserved catalytic domain and reduced auxiliary domains. The {alpha}-glucosidase, a member of GH31 family, shows substrate preference for {alpha}(1-6) over {alpha}(1-4) glycosidic linkages and produces glucose from isomaltose as well as maltose. The preference can be switched by a single mutation at its active site, suggestive of widespread adaptation to utilization of a variety of polysaccharides by intestinal micro-organisms as energy resources. Novel {alpha}-glucosidase from human gut microbiome: substrate specificities and their switch.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Institutes of Health (NIH); USDOE Office of Science (SC)
OSTI Identifier:
991103
Report Number(s):
ANL/BIO/JA-68190
Journal ID: 0892-6638; TRN: US201020%%740
DOE Contract Number:  
DE-AC02-06CH11357
Resource Type:
Journal Article
Journal Name:
The FASEB J.
Additional Journal Information:
Journal Volume: 24; Journal Issue: 2010
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; CARBOHYDRATES; CRYSTAL STRUCTURE; ENZYMES; GENES; GLUCOSE; GLYCOSIDES; HYDROLASES; INTESTINES; MALTOSE; METABOLISM; MUTANTS; MUTATIONS; PATHOLOGY; PHYSIOLOGY; POLYSACCHARIDES; PROTEIN STRUCTURE; PROTEINS; SUBSTRATES

Citation Formats

Tan, K., Tesar, C., Wilton, R., Keigher, L., Babnigg, G., Joachimiak, A., and Biosciences Division. Novel {alpha}-glucosidase from human gut microbiome : substrate specificities and their switch.. United States: N. p., 2010. Web. doi:10.1096/fj.10-156257.
Tan, K., Tesar, C., Wilton, R., Keigher, L., Babnigg, G., Joachimiak, A., & Biosciences Division. Novel {alpha}-glucosidase from human gut microbiome : substrate specificities and their switch.. United States. doi:10.1096/fj.10-156257.
Tan, K., Tesar, C., Wilton, R., Keigher, L., Babnigg, G., Joachimiak, A., and Biosciences Division. Fri . "Novel {alpha}-glucosidase from human gut microbiome : substrate specificities and their switch.". United States. doi:10.1096/fj.10-156257.
@article{osti_991103,
title = {Novel {alpha}-glucosidase from human gut microbiome : substrate specificities and their switch.},
author = {Tan, K. and Tesar, C. and Wilton, R. and Keigher, L. and Babnigg, G. and Joachimiak, A. and Biosciences Division},
abstractNote = {The human intestine harbors a large number of microbes forming a complex microbial community that greatly affects the physiology and pathology of the host. In the human gut microbiome, the enrichment in certain protein gene families appears to be widespread. They include enzymes involved in carbohydrate metabolism such as glucoside hydrolases of dietary polysaccharides and glycoconjugates. We report the crystal structures (wild type, 2 mutants, and a mutant/substrate complex) and the enzymatic activity of a recombinant {alpha}-glucosidase from human gut bacterium Ruminococcus obeum. The first ever protein structures from this bacterium reveal a structural homologue to human intestinal maltase-glucoamylase with a highly conserved catalytic domain and reduced auxiliary domains. The {alpha}-glucosidase, a member of GH31 family, shows substrate preference for {alpha}(1-6) over {alpha}(1-4) glycosidic linkages and produces glucose from isomaltose as well as maltose. The preference can be switched by a single mutation at its active site, suggestive of widespread adaptation to utilization of a variety of polysaccharides by intestinal micro-organisms as energy resources. Novel {alpha}-glucosidase from human gut microbiome: substrate specificities and their switch.},
doi = {10.1096/fj.10-156257},
journal = {The FASEB J.},
number = 2010,
volume = 24,
place = {United States},
year = {2010},
month = {1}
}