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Maitake, Hen of the Woods · 2004 · Journal Article

High relevance

Purification and Characterization of a Novel Prolyl Aminopeptidase from Maitake (Grifola frondosa)

Grifola frondosa

Immune support
SpeciesMaitake, Hen of the Woods
JournalBioscience, biotechnology, and biochemistry
Year2004

Key points

  • 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

Metadata-grounded summary

Citation 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.

Citation

Hiwatashi K, Hori K, Takahashi K, Kagaya A, Inoue S, Sugiyama T, et al. (2004). Purification and Characterization of a Novel Prolyl Aminopeptidase from Maitake (Grifola frondosa). Bioscience, biotechnology, and biochemistry https://doi.org/10.1271/bbb.68.1395 PMID: 15215614

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