Characterization of the pro-aminopeptidase from Aeromonas caviae T-64.
The pro-aminopeptidase from Aeromonas caviae T-64 (pro-apAC) had maximal activity at 60 degrees C and was more stable than mature apAC at temperature up to 65 degrees C for 1 hour. The pH stability of pro-apAC ranged from 4.0 to 8.0, which is broader than the range for the mature apAC. The kcat/Km of pro-apAC was 1.4% to 24% of that of mature apAC.
Zhang
Z Z
ZZ
Applied Enzymology Laboratory, National Food Research Institute, Tsukuba, Ibaraki, Japan.
Nirasawa
S
S
Nakajima
Y
Y
Yoshida
M
M
Kusakabe
I
I
Hayashi
K
K
D000333:Aeromonas / Q000201:enzymology*; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D009842:Oligopeptides; D010618:Phenanthrolines / Q000494:pharmacology; D013379:Substrate Specificity
D004792:Enzyme Precursors; D009842:Oligopeptides; D010618:Phenanthrolines; D004492:Edetic Acid; D000626:Aminopeptidases; D007930:Leucine; C012211:ubenimex; C025205:1,10-phenanthroline