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

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

12 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 language	English
Pages (from-to)	319-323
Number of pages	5
Journal	Phytochemistry
Volume	53
Issue number	3
DOIs	https://doi.org/10.1016/S0031-9422(99)00534-8
Publication status	Published - 2000 Feb 2
Externally published	Yes

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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10.1016/S0031-9422(99)00534-8

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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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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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JO - Phytochemistry

JF - Phytochemistry

SN - 0031-9422

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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