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From the same journal

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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Published copy (DOI)

Author(s)

  • R. Suresh Kumar
  • James A. Brannigan
  • Asmita A. Prabhune
  • Archana V. Pundle
  • Guy G. Dodson
  • Eleanor J. Dodson
  • C. G. Suresh

Department/unit(s)

Publication details

JournalJournal of Biological Chemistry
DatePublished - 27 Oct 2006
Issue number43
Volume281
Number of pages10
Pages (from-to)32516-32525
Original languageEnglish

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 alpha beta beta alpha 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.

    Research areas

  • LACTIC-ACID BACTERIA, QUANTITATIVE-DETERMINATION, LACTOBACILLUS-PLANTARUM, CHOLESTEROL, DECONJUGATION, PURIFICATION, CLONING, EXPRESSION, GENE

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