01980nas a2200217   4500008004100000022001400041245016600055210006900221260010300290300001600393490000800409520106400417100001801481700002501499700002101524700002401545700002001569700002401589700001901613856013001632       2006                        eng d  a0021-925800aStructural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase0 aStructural and functional analysis of a conjugated bile salt hyd  a9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USAbAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCcOCT  a32516-325250 v2813 a<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>1 aKumar, Suresh1 aBrannigan, James, A.1 aPrabhune, Asmita1 aPundle, Archana, V.1 aDodson, Guy, G.1 aDodson, Eleanor, J.1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/structural-and-functional-analysis-conjugated-bile-salt-hydrolase-bifidobacterium-longum-001476nas a2200289   4500008004100000022001400041245011400055210006900169260007600238300001200314490000700326520044800333653002000781653002200801653001900823653002200842653002000864653002000884100002900904700001800933700001900951700002100970700002000991700002401011700001901035856013201054       2012                        eng d  a1744-309100aCrystallization and X-ray structure analysis of a thermostable penicillin G acylase from alcaligenes faecalis0 aCrystallization and Xray structure analysis of a thermostable pe  aCOMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USAbWILEY-BLACKWELLcMAR  a273-2770 v683 a<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>10acalcium binding10adisulfide bridges10aNtn hydrolases10aorthorhombic form10atetragonal form10aThermostability1 aVarshney, Nishant, Kumar1 aKumar, Suresh1 aIgnatova, Zoya1 aPrabhune, Asmita1 aPundle, Archana1 aDodson, Eleanor, J.1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/crystallization-and-x-ray-structure-analysis-thermostable-penicillin-g-acylase-alcaligenes-0