Acyl-CoA: 6-APA acyltransferase from Penicillium chrysogenum studies on its hydrolytic activity.
Acyl-CoA: 6-APA acyltransferase (AT) from Penicillium chrysogenum Wis 54-1255 catalyzes the hydrolysis of different acyl-CoA derivatives generating, in the absence of 6-APA, free acid and CoA. The hydrolytic efficiency of AT is highest for acyl-CoA variants in which the acyl-moiety is higher than six carbon atoms. The maximal rate of catalysis was achieved in 50 mM Tris-HCl buffer, pH 8.5 at 35 degrees C. Unlike the AT activity, the acylase activity has a different optimum temperature and substrate specificity and dithiothreitol is not required for the reaction.
Martín-Villacorta
J
J
Departmento Interfacultativo de Bioquímica y Biología Molecular, Facultades de Biología y Veterinaria, Universidad de León, España.
Reglero
A
A
Luengo
J M
JM
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000217:Acyltransferases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010397:Penicillanic Acid / Q000378:metabolism* / Q000031:analogs & derivatives; D046915:Penicillin-Binding Proteins; D010408:Penicillium chrysogenum / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
D000214:Acyl Coenzyme A; D046915:Penicillin-Binding Proteins; D010397:Penicillanic Acid; D000217:Acyltransferases; C018756:acyl-CoA-6-aminopenicillanic acid acyltransferase; C004408:aminopenicillanic acid