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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
Open accessAbstract
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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“the terminal cysteine Cys1 of BlBSH is predicted to be the primary catalytic residue, although other active site residues (for example, Thr2, Trp21, Thr171, Asn172 and Arg225) may also be important for BSH activity or substrate specificity24.”
From Bile Acids Are Substrates for Amine N-Acyl Transferase Activity by Bile Salt Hydrolase (2022) · cites this paper as [24]
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Metadata
- 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.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-10
- Volume
- 281
- Issue
- 43
- Pages
- 32516-32525
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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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