<?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%">Chandra, P. M.</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, A.</style></author><author><style face="normal" font="default" size="100%">Turkenburg, J. P.</style></author><author><style face="normal" font="default" size="100%">Dodson, Guy G.</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%">Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Crystallographica Section F-Structural Biology and Crystallization Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">BLACKWELL PUBLISHING</style></publisher><pub-location><style face="normal" font="default" size="100%">9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">61</style></volume><pages><style face="normal" font="default" size="100%">124-127</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">Part 1</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><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%">0.647</style></custom4></record><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%">Rathinaswamy, P.</style></author><author><style face="normal" font="default" size="100%">Pundle, A. V.</style></author><author><style face="normal" font="default" size="100%">Prabhune, Asmita</style></author><author><style face="normal" font="default" size="100%">SivaRaman, H.</style></author><author><style face="normal" font="default" size="100%">Brannigan, James A.</style></author><author><style face="normal" font="default" size="100%">Dodson, Guy G.</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%">Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Crystallographica Section F-Structural Biology Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">7</style></number><publisher><style face="normal" font="default" size="100%">INT UNION CRYSTALLOGRAPHY</style></publisher><pub-location><style face="normal" font="default" size="100%">2 ABBEY SQ, CHESTER, CH1 2HU, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">61</style></volume><pages><style face="normal" font="default" size="100%">680-683</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;{Penicillin acylase proteins are amidohydrolase enzymes that cleave penicillins at the amide bond connecting the side chain to their beta-lactam nucleus. An unannotated protein from Bacillus subtilis has been expressed in Escherichia coli, purified and confirmed to possess penicillin V acylase activity. The protein was crystallized using the hanging-drop vapour-diffusion method from a solution containing 4 M sodium formate in 100 mM Tris-HCl buffer pH 8.2. Diffraction data were collected under cryogenic conditions to a spacing of 2.5 A. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 111.0&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">Part 7</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><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%">0.647</style></custom4></record><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><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%">Suresh, C. G.</style></author><author><style face="normal" font="default" size="100%">Brannigan, James A.</style></author><author><style face="normal" font="default" size="100%">Dodson, Guy G.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Bile salt hydrolase, the member of Ntn-hydrolase family: differential modes of structural and functional transitions during denaturation</style></title><secondary-title><style face="normal" font="default" size="100%">IUBMB Life</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aggregation</style></keyword><keyword><style  face="normal" font="default" size="100%">Bile salt hydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">molten-globule</style></keyword><keyword><style  face="normal" font="default" size="100%">Unfolding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">2</style></number><publisher><style face="normal" font="default" size="100%">TAYLOR &amp; FRANCIS INC</style></publisher><pub-location><style face="normal" font="default" size="100%">325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USA</style></pub-location><volume><style face="normal" font="default" size="100%">59</style></volume><pages><style face="normal" font="default" size="100%">118-125</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Conformational transitions and functional stability of the bile salt hydrolase (BSH; cholylglycine EC: 3.5.1.24) from Bifidobacterium longum (BlBSH) cloned and expressed in E. coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and CD spectroscopy. Thermal and Gdn-HCl-mediated denaturation of BlBSH is a multistep process of inactivation and unfolding. The inactivation and unfolding of the enzyme was found to be irreversible. Enzyme activity seems sensitive to even minor conformational changes at the active site. Thermal denaturation as such did not result in any insoluble protein aggregates. However, on treating with 0.25-1 M Gdn-HCl the enzyme showed increasing aggregation at temperatures of 40-55 degrees C indicating more complex structural changes taking place in the presence of chemical denaturants. The enzyme secondary structure was still intact at acidic pH (pH 1-3). The perturbation in the tertiary structure at the acidic pH was detected through freshly formed solvent exposed hydrophobic patches on the enzyme. These changes could be due to the formation of an acid-induced molten globule-like state.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.653</style></custom4></record><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%">Rathinaswamy, Priya</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author><author><style face="normal" font="default" size="100%">Suresh, C. G.</style></author><author><style face="normal" font="default" size="100%">Prabhune, Asmita</style></author><author><style face="normal" font="default" size="100%">Brannigan, James A.</style></author><author><style face="normal" font="default" size="100%">Dodson, Guy G.</style></author><author><style face="normal" font="default" size="100%">Pundle, Archana V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purification and characterization of YxeI, a penicillin acylase from Bacillus subtilis</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bacillus subtilis</style></keyword><keyword><style  face="normal" font="default" size="100%">Conjugated bile acid hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Ntn hydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillin acylase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">50</style></volume><pages><style face="normal" font="default" size="100%">25-30</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The paper reports the purification and characterization of the first penicillin acylase from Bacillus subtilis. YxeI, the protein annotated as hypothetical, coded by the gene yxeI in the open reading frame between iol and hut operons in B. subtilis was cloned and expressed in Eshcherichia coli, purified and characterized. The purified protein showed measurable penicillin acylase activity with penicillin V. The enzyme was a homotetramer of 148 kDa. The apparent Km of the enzyme for penicillin V and the synthetic substrate 2-nitro-5-(phenoxyacetamido)-benzoic acid was 40 mM and 0.63 mM, respectively, and the association constants were 8.93 x 10(2) M-1 and 2.51 x 10(5) M-1, respectively. It was inhibited by cephalosporins and conjugated bile salts, substrates of the closely related bile acid hydrolases. It had good sequence homology with other penicillin V acylases and conjugated bile acid hydrolases, members of the Ntn hydrolase family. The N-terminal nucleophile was a cysteine which is revealed by a simple removal of N-formyl-methionine. The activity of the protein was affected by high temperature, acidic pH and the presence of the denaturant guanidine hydrochloride. (C) 2011 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.596
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