<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kumar, R. Suresh</style></author><author><style face="normal" font="default" size="100%">Brannigan, James A.</style></author><author><style face="normal" font="default" size="100%">Prabhune, Asmita</style></author><author><style face="normal" font="default" size="100%">Pundle, Archana V.</style></author><author><style face="normal" font="default" size="100%">Dodson, Guy G.</style></author><author><style face="normal" font="default" size="100%">Dodson, Eleanor J.</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Biological Chemistry</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">43</style></number><publisher><style face="normal" font="default" size="100%">AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC</style></publisher><pub-location><style face="normal" font="default" size="100%">9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA</style></pub-location><volume><style face="normal" font="default" size="100%">281</style></volume><pages><style face="normal" font="default" size="100%">32516-32525</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">4.258</style></custom4></record></records></xml>