2hez

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[[Image:2hez.gif|left|200px]]
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{{Seed}}
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[[Image:2hez.png|left|200px]]
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{{STRUCTURE_2hez| PDB=2hez | SCENE= }}
{{STRUCTURE_2hez| PDB=2hez | SCENE= }}
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'''Bifidobacterium longum bile salt hydrolase'''
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===Bifidobacterium longum bile salt hydrolase===
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==Overview==
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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 line below this paragraph, {{ABSTRACT_PUBMED_16905539}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16905539 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16905539}}
==About this Structure==
==About this Structure==
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[[Category: Alpha]]
[[Category: Alpha]]
[[Category: Beta]]
[[Category: Beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:12:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:20:41 2008''

Revision as of 01:20, 29 July 2008

Image:2hez.png

Template:STRUCTURE 2hez

Bifidobacterium longum bile salt hydrolase

Template:ABSTRACT PUBMED 16905539

About this Structure

2HEZ 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

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