Cited by 40Steroid Chemistry and BiochemistryEnzyme Production and CharacterizationGut microbiota and health

Functional and Phylogenetic Diversity of BSH and PVA Enzymes

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Daly, Jack W., Keely, Stephen J., Gahan, Cormac G. M.·2021·Microorganisms

Abstract

Bile salt hydrolase (BSH) and penicillin V acylase (PVA) are related enzymes that are classified as choloylglycine hydrolases (CGH). BSH enzymes have attracted significant interest for their ability to modulate the composition of the bile acid pool, alter bile acid signaling events mediated by the host bile acid receptors FXR and TGR5 and influence cholesterol homeostasis in the host, while PVA enzymes have been widely utilised in an industrial capacity in the production of semi-synthetic antibiotics. The similarities between BSH and PVA enzymes suggest common evolution of these enzymes and shared mechanisms for substrate binding and catalysis. Here, we compare BSH and PVA through analysis of the distribution, phylogeny and biochemistry of these microbial enzymes. The development of new annotation approaches based upon functional enzyme analyses and the potential implications of BSH enzymes for host health are discussed.

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Crossref · 10.3390/microorganisms9040732

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  • BSH and PVA are evolutionary related enzymes with high similarity in the amino acid residues involved in their active site.

    “BSH and PVA are evolutionary related enzymes with high similarity in terms of the amino acid residues involved in their active site [5, 84].”

    From Bile Salt Hydrolase Activity in the Food-Derived Strain Levilactobacillus brevis M3R3: Genomic and Functional Characterization (2026) · cites this paper as [84]

    The Introduction and §3.2 describe BSH and PVA as likely evolutionarily related and report that five of six major catalytic residues are conserved. The active-site similarity is supported, but the claim states their evolutionary relationship as fact where the paper presents it as likely. Page numbers were not supplied. (LLM, conf=0.88)

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Authors
Daly, J. W., Keely, S. J., & Gahan, C. G. M.
Affiliations
  • University College Cork (IE)
  • Royal College of Surgeons in Ireland (IE)
Corresponding author
Gahan, Cormac G. M.
Venue
Microorganisms
Publisher
MDPI AG
Published
2021-03-31
Volume
9
Issue
4
Pages
732
ISSN
2076-2607 (ISSN-L)
OpenAlex
W3152258656
Cited by
40
References
90
Citations by year
2026: 7 · 2025: 7 · 2024: 8 · 2023: 7 · 2022: 9 · 2021: 2
FWCI
0.68
Type
journal article
Language
en
Open access
Locations
  • Microorganisms (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Figshare (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Science Foundation Ireland (16/IA/4445)
  • APC Microbiome Ireland (SFI/12/RC/2273)
  • Irish Department of Agriculture Food and the Marine (DAFM) under the Food Institutional Re-search Measure (FIRM) (17F244)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gut microbiota and health
Keywords
bile salt hydrolase, penicillin V acylase, enzyme phylogeny, functional diversity, bile acid metabolism, farnesoid X receptor, TGR5, cholesterol homeostasis, semisynthetic antibiotics, enzyme evolution, microbial enzymes

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