Purification and characterization of a novel prolyl aminopeptidase from Maitake (Grifola frondosa).
We have found a novel prolyl aminopeptidase in Grifola frondosa. The enzyme was purified by DEAE-Sepharose CL-6B, Butyl-Toyopearl, Sephacryl S-100, and Mono-Q column chromatographies. The purified enzyme exists as a dimer and gives high activity toward L-proline-p-nitroanilide. The enzyme was strongly inhibited by p-chloromercuribenzoic acid and iodoacetic acid and markedly inhibited by phenylmethylsulfonyl fluoride and arphamenin A.
Hiwatashi
Kazuyuki
K
Department of Bioengineering, Akita Research Institute of Food and Brewing, Akita, Japan.
Hori
Kazuyuki
K
Takahashi
Keitaro
K
Kagaya
Akira
A
Inoue
Shunzo
S
Sugiyama
Toshihiro
T
Takahashi
Saori
S
D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D019281:Dimerization; D004151:Dipeptides / Q000378:metabolism; D004791:Enzyme Inhibitors; D048691:Grifola / Q000737:chemistry / Q000201:enzymology*; D007700:Kinetics; D013379:Substrate Specificity
D004151:Dipeptides; D004791:Enzyme Inhibitors; D000626:Aminopeptidases; C022450:prolyl aminopeptidase