Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts.
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.
Dean
Mariangela
M
Department of Biochemistry and Molecular Biology, University of Ferrara, 44100 Ferrara, Italy.
Cervellati
Carlo
C
Casanova
Elena
E
Squerzanti
Monica
M
Lanzara
Vincenzo
V
Medici
Alessandro
A
Polverino De Laureto
Patrizia
P
Bergamini
Carlo M
CM
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
D001647:Bile Acids and Salts; D013656:Taurocholic Acid; D000581:Amidohydrolases; C023154:choloylglycine hydrolase; D006000:Glycocholic Acid