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'''Bifidobacterium longum bile salt hydrolase''' | '''Bifidobacterium longum bile salt hydrolase''' | ||
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[[Category: Kumar, R S.]] | [[Category: Kumar, R S.]] | ||
[[Category: Suresh, C G.]] | [[Category: Suresh, C G.]] | ||
[[Category: | [[Category: Alpha]] | ||
[[Category: | [[Category: Beta]] | ||
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Revision as of 03:12, 4 May 2008
Bifidobacterium longum bile salt hydrolase
Overview
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.
About this Structure
2HF0 is a Single protein structure of sequence from Bifidobacterium longum. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase., Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG, J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:16905539 Page seeded by OCA on Sun May 4 06:12:53 2008
