Purification and characterization of a novel prolyl aminopeptidase from Maitake (Grifola frondosa).

Kazuyuki Hiwatashi, Kazuyuki Hori, Keitaro Takahashi, Akira Kagaya, Shunzo Inoue, Toshihiro Sugiyama, Saori Takahashi

Index: Biosci. Biotechnol. Biochem. 68 , 1395-7, (2004)

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Abstract

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.