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