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Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase

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Kumar, R. Suresh, Brannigan, James A., Prabhune, Asmita A., Pundle, Archana V., Dodson, Guy G., Dodson, Eleanor J., Suresh, C.G.·2006·Journal of Biological Chemistry

DOI 10.1074/jbc.m604172200

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Abstract

Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alphabetabetaalpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.

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Authors: Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J., & Suresh, C. G.
Affiliations: National Chemical Laboratory (IN)
University of York (GB)
Corresponding author: Brannigan, James A.
Suresh, C.G.
ORCID: Kumar, R. Suresh
Brannigan, James A.
Prabhune, Asmita A.
Dodson, Eleanor J.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2006-10
Volume: 281
Issue: 43
Pages: 32516-32525
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m604172200
OpenAlex: W1998273216
Cited by: 143
References: 43
Citations by year: 2026: 3 · 2025: 3 · 2024: 10 · 2023: 9 · 2022: 12 · 2021: 13 · 2020: 12 · 2019: 10 · 2018: 11 · 2017: 6 · 2016: 8 · 2015: 8 · 2014: 6 · 2013: 7 · 2012: 3
FWCI: 3.49
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5104 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Wellcome Trust
Council of Scientific and Industrial Research, India
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: bile salt hydrolase, Bifidobacterium longum, penicillin V acylase, enzyme crystal structure, zymogen activation, substrate specificity, enzyme kinetics, enzyme evolution, Clostridium perfringens, Bacillus sphaericus, gut microbiota, bile acid deconjugation
MeSH terms: Amidohydrolases, Amino Acid Sequence, Bifidobacterium, Binding Sites, Clostridium perfringens, Hydrogen Bonding, Kinetics, Models, Molecular, Molecular Sequence Data, Penicillin Amidase, Protein Binding, Protein Conformation, Spectrometry, Fluorescence, Substrate Specificity, Molecular Structure, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Protein Structure, Secondary, Crystallography, X-Ray, Evolution, Molecular, Dimerization, Protein Structure, Quaternary, Static Electricity, Hydrophobic and Hydrophilic Interactions

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Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase

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