@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.}
}
@article { ISI:000301921300006,
	title = {Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis},
	journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications},
	volume = {68},
	number = {3},
	year = {2012},
	month = {MAR},
	pages = {273-277},
	publisher = {WILEY-BLACKWELL},
	address = {COMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USA},
	abstract = {<p>{The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C2221, with unit-cell parameters a = 72.9</p>},
	keywords = {calcium binding, disulfide bridges, Ntn hydrolases, orthorhombic form, tetragonal form, Thermostability},
	issn = {1744-3091},
	doi = {10.1107/S1744309111053930},
	author = {Varshney, Nishant Kumar and Kumar, R. Suresh and Ignatova, Zoya and Prabhune, Asmita and Pundle, Archana and Dodson, Eleanor J. and Suresh, C. G.}
}
