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

doi:10.1016/S0031-9422(99)00534-8

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)

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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
巻	53
号	3
DOI	https://doi.org/10.1016/S0031-9422(99)00534-8
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

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10.1016/S0031-9422(99)00534-8

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

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.",

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author = "Yukiko Utsunomiya and Toru Nakayama and Hideo Oohira and Rie Hirota and Terutoshi Mori and Fusako Kawai and Takashi Ueda",

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T1 - Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds

AU - Utsunomiya, Yukiko

AU - Nakayama, Toru

AU - Oohira, Hideo

AU - Hirota, Rie

AU - Mori, Terutoshi

AU - Kawai, Fusako

AU - Ueda, Takashi

PY - 2000/2/2

Y1 - 2000/2/2

N2 - 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.

AB - 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.

KW - Allene oxide synthase

KW - Corn

KW - Cytochrome P450

KW - Inactivation

KW - Poaceae

KW - Zea mays

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DO - 10.1016/S0031-9422(99)00534-8

M3 - Article

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AN - SCOPUS:0034142039

VL - 53

SP - 319

EP - 323

JO - Phytochemistry

JF - Phytochemistry

SN - 0031-9422

IS - 3

ER -

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

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