@article { ISI:000241414500049,
	title = {Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase},
	journal = {Journal of Biological Chemistry},
	volume = {281},
	number = {43},
	year = {2006},
	month = {OCT},
	pages = {32516-32525},
	publisher = {AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC},
	address = {9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA},
	abstract = {<p>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 alpha beta beta alpha 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.</p>},
	issn = {0021-9258},
	doi = {10.1074/jbc.M604172200},
	author = {Kumar, R. Suresh and Brannigan, James A. and Prabhune, Asmita and Pundle, Archana V. and Dodson, Guy G. and Dodson, Eleanor J. and Suresh, C. G.}
}
