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PMID: 12039776 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts.

Applied and environmental microbiology ·Vol. 68 ·No. 6 ·2002-06-00 ·Pages 3126-8

Dean M, Cervellati C, Casanova E, Squerzanti M, Lanzara V, Medici A, Polverino De Laureto P, Bergamini CM

Abstract

Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60 degrees C for up to 60 min, in agreement with calorimetric data.

MeSH Terms
Amidohydrolases/metabolism Animals Bile/metabolism Bile Acids and Salts/metabolism Cattle Glycocholic Acid/metabolism Hydrolysis Stenotrophomonas maltophilia/enzymology Taurocholic Acid/metabolism
Chemicals
Bile Acids and Salts Taurocholic Acid Amidohydrolases choloylglycine hydrolase Glycocholic Acid
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Dean Mariangela
Department of Biochemistry and Molecular Biology, University of Ferrara, 44100 Ferrara, Italy.
Cervellati Carlo
Casanova Elena
Squerzanti Monica
Lanzara Vincenzo
Medici Alessandro
Polverino De Laureto Patrizia
Bergamini Carlo M
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Article Info
Journal
Applied and environmental microbiology
Abbr.
Appl Environ Microbiol
ISSN
0099-2240
DOI
10.1128/AEM.68.6.3126-3128.2002
Published
2002-06-00
Pages
3126-8
Language
English
Region
United States
NLM ID
7605801
PMCID
PMC123940
Subset
IM
External Links
PubMed source DOI: 10.1128/AEM.68.6.3126-3128.2002 PMC Full Text View journal details
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