2hf0
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(New page: 200px<br /><applet load="2hf0" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hf0, resolution 2.30Å" /> '''Bifidobacterium long...)
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Revision as of 18:19, 29 January 2008
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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. Active as Choloylglycine hydrolase, with EC number 3.5.1.24 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
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