[Partial characterization of 2 extracellular aminopeptidases (arylamidases) from the dermatophyte Keratinomyces ajelloi].
Two aminopeptidases AP1 and AP2 have been isolated from Keratinomyces ajelloi filtrates. The molecular weight is about 27 000 for AP1 and 23 000 for AP2. Both aminopeptidases present maximum activity at pH 9.35 but 50 p. 100 of maximum activity is observed between pH 7.5 and pH 8.5. Km values measured at pH 9.35 with L-leucine-p-nitroanilide as substrate are 0.38 X 10(-3) M for AP1 and 0.43 X 10(-3) M for AP2. kcat at the same pH are 63.6 sec.-1 for AP-1 and 62.8 sec-1 for AP2. Both aminopeptidases are inhibited by mercuric chloride, o-phenanthroline, dithiothreitol and 2-mercaptoethanol. Some of their characters make them similar to Streptomyces griseus pronase aminopeptidases.
D000626:Aminopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D003883:Arthrodermataceae / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight
D000626:Aminopeptidases
Caractérisation partielle de deux aminopeptidases (arylamidases) extracellulaires du dermatophyte Keratinomyces ajelloi.