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

研究成果: Article査読

12 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)319-323
ページ数5
ジャーナルPhytochemistry
53
3
DOI
出版ステータスPublished - 2000 2月 2
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 植物科学
  • 園芸学

フィンガープリント

「Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル