Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds

Yukiko Utsunomiya, Toru Nakayama, Hideo Oohira, Rie Hirota, Terutoshi Mori, Fusako Kawai, Takashi Ueda

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

The allene oxide synthase (AOS) was purified from corn (Zea mays) seeds to homogeneity and characterized partially. The corn AOS was a hemoprotein cytochrome P450 with a molecular weight and pI of 53,000 and 6.0, respectively. The corn AOS was found to be irreversibly inactivated by a substrate, 13-hydroperoxyoctadienoic acid. The rate of the enzyme inactivation was higher at low pHs. (C) 2000 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)319-323
Number of pages5
JournalPhytochemistry
Volume53
Issue number3
DOIs
Publication statusPublished - 2000 Feb 2
Externally publishedYes

Keywords

  • Allene oxide synthase
  • Corn
  • Cytochrome P450
  • Inactivation
  • Poaceae
  • Zea mays

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture

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