[Hydrolysis of N-acetyl-L- and N-acetyl-D,L-methionine by microbial aminacylase].
The kinetics of N-acetyl-L- and N-acetyl-D,L-methionine hydrolysis by aminoacylase from Asp. oryzae were studied. The maximal rate of the reaction was found to be about 2000 mu moles of L-methionine per mg of protein per hour; Km was equal to about 1.10(-1) M for both the racemic and optically active substrates. In the presence of Co(II) ions (the molar ratio of N-acetyl-L-methionine/Co(II) was 100:1) the reaction velocity was increased. The values of approximately 4500 and approximately 3000 mu moles per mg per hour were-attained with L-enantiomer and racemic substrates, respectively. The Km values were decreased down to 2.10(-2) M and 1.4.10(-2) M, respectively.
D000581:Amidohydrolases / Q000378:metabolism*; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D007700:Kinetics; D008715:Methionine / Q000031:analogs & derivatives*; D013237:Stereoisomerism; D013379:Substrate Specificity
C006379:N-acetylmethionine; D008715:Methionine; D000581:Amidohydrolases; C019672:aminoacylase I
Gidroliz N-atsetil-L i N-atsetil-D,L-metionina mikrobnoĩ aminoatsilazoĩ.