2hf0: Difference between revisions

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==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.

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==

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[[Category: Choloylglycine hydrolase]]

[[Category: Single protein]]

[[Category: Brannigan, J.A.]]

[[Category: Brannigan, J A.]]

[[Category: Kumar, R.S.]]

[[Category: Kumar, R S.]]

[[Category: Suresh, C.G.]]

[[Category: Suresh, C G.]]

[[Category: alpha]]

[[Category: beta]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:09 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Choloylglycine hydrolase]]
 [[Category: Single protein]]
-[[Category: Brannigan, J.A.]]
+[[Category: Brannigan, J A.]]
-[[Category: Kumar, R.S.]]
+[[Category: Kumar, R S.]]
-[[Category: Suresh, C.G.]]
+[[Category: Suresh, C G.]]
 [[Category: alpha]]
 [[Category: beta]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:19:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:09 2008''