2HEZ

Bifidobacterium longum bile salt hydrolase

Summary for 2HEZ

• Entry DOI: 10.2210/pdb2hez/pdb
• Related: 2HF0
• Descriptor: Bile salt hydrolase, SULFATE ION (3 entities in total)
• Functional Keywords: alpha, beta, hydrolase
• Biological source: Bifidobacterium longum
• Total number of polymer chains: 2
• Total formula weight: 70301.62

Authors

Suresh, C.G.,Kumar, R.S.,Brannigan, J.A. (deposition date: 2006-06-22, release date: 2006-09-19, Last modification date: 2023-11-15)

Primary citation

Kumar, R.S.,Brannigan, J.A.,Prabhune, A.A.,Pundle, A.V.,Dodson, G.G.,Dodson, E.J.,Suresh, C.G.
Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase.
J.Biol.Chem., 281:32516-32525, 2006

PubMed Abstract: 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.

PubMed: 16905539
DOI: 10.1074/jbc.M604172200

Experimental method

X-RAY DIFFRACTION (2.5 Å)