Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase
| Autor: | Cheravakkattu G. Suresh, Guy Dodson, Archana Pundle, R. Suresh Kumar, Eleanor J. Dodson, James A. Brannigan, Asmita Prabhune |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Bifidobacterium longum Clostridium perfringens Protein Conformation Stereochemistry Molecular Sequence Data Static Electricity Crystallography X-Ray Biochemistry Bacillus sphaericus Protein Structure Secondary Amidohydrolases Substrate Specificity Evolution Molecular Clostridium Zymogen Hydrolase Amino Acid Sequence Protein Structure Quaternary Molecular Biology chemistry.chemical_classification Binding Sites Molecular Structure Sequence Homology Amino Acid biology Hydrogen Bonding Cell Biology biology.organism_classification Protein tertiary structure Kinetics Spectrometry Fluorescence Enzyme chemistry Glycine Mutagenesis Site-Directed Bifidobacterium Penicillin Amidase Dimerization Hydrophobic and Hydrophilic Interactions Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 281:32516-32525 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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