2hf0
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | Bile salt hydrolase (BSH) is an enzyme produced by the intestinal | + | 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== | ==About this Structure== | ||
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[[Category: Choloylglycine hydrolase]] | [[Category: Choloylglycine hydrolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brannigan, J | + | [[Category: Brannigan, J A.]] |
| - | [[Category: Kumar, R | + | [[Category: Kumar, R S.]] |
| - | [[Category: Suresh, C | + | [[Category: Suresh, C G.]] |
[[Category: alpha]] | [[Category: alpha]] | ||
[[Category: beta]] | [[Category: beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:09 2008'' |
Revision as of 15:41, 21 February 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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