A kinetic study into the hydrolysis of the ochratoxins and analogues by carboxypeptidase A.
The hydrolyses of the ochratoxins and analogues by carboxypeptidase A were assessed. This was done by measuring the amount of phenylalanine formed with liquid chromatography coupled to tandem electrospray mass spectrometry. The kinetic data of ochratoxin A, ochratoxin B, and the synthetic bromo-ochratoxin B were compared to the values of a number of synthesized structure analogues, namely, ochratoxin A methyl ester, ochratoxin B methyl ester, N-(2-hydroxybenzoyl)phenylalanine, N-(5-chloro-2-hydroxybenzoyl)phenylalanine, N-(5-bromo-2-hydroxybenzoyl)phenylalanine, and N-(5-fluoro-2-hydroxybenzoyl)phenylalanine. The halogen-containing analogues had lower turnovers than their des-halo analogues. There are no substantial differences in the kinetic data between the different halogen-containing analogues.
Stander
M A
MA
Potchefstroom University for Christian Higher Education, Potchefstroom, South Africa.
Steyn
P S
PS
van Der Westhuizen
F H
FH
Payne
B E
BE
D002268:Carboxypeptidases / Q000378:metabolism*; D043422:Carboxypeptidases A; D006219:Halogens / Q000737:chemistry; D006868:Hydrolysis; D007700:Kinetics; D009793:Ochratoxins / Q000737:chemistry* / Q000378:metabolism; D010649:Phenylalanine
D006219:Halogens; D009793:Ochratoxins; D010649:Phenylalanine; D002268:Carboxypeptidases; D043422:Carboxypeptidases A