title: Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts.
abstract: Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60 degrees C for up to 60 min, in agreement with calorimetric data.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Ferrara, 44100 Ferrara, Italy.
authors.forename: Mariangela
authors.initials: M
authors.lastname: Dean
authors.forename: Carlo
authors.initials: C
authors.lastname: Cervellati
authors.forename: Elena
authors.initials: E
authors.lastname: Casanova
authors.forename: Monica
authors.initials: M
authors.lastname: Squerzanti
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Lanzara
authors.forename: Alessandro
authors.initials: A
authors.lastname: Medici
authors.forename: Patrizia
authors.initials: P
authors.lastname: Polverino De Laureto
authors.forename: Carlo M
authors.initials: CM
authors.lastname: Bergamini
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D001646:Bile / Q000378:metabolism; D001647:Bile Acids and Salts / Q000378:metabolism*; D002417:Cattle; D006000:Glycocholic Acid / Q000378:metabolism; D006868:Hydrolysis; D020615:Stenotrophomonas maltophilia / Q000201:enzymology*; D013656:Taurocholic Acid / Q000378:metabolism
chemical_list: D001647:Bile Acids and Salts; D013656:Taurocholic Acid; D000581:Amidohydrolases; C023154:choloylglycine hydrolase; D006000:Glycocholic Acid