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.
authors.affiliation: Faculty of Nutrition, Kobe Gakuin University, Hyogo, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Utsunomiya
authors.forename: T
authors.initials: T
authors.lastname: Nakayama
authors.forename: H
authors.initials: H
authors.lastname: Oohira
authors.forename: R
authors.initials: R
authors.lastname: Hirota
authors.forename: T
authors.initials: T
authors.lastname: Mori
authors.forename: F
authors.initials: F
authors.lastname: Kawai
authors.forename: T
authors.initials: T
authors.lastname: Ueda
mesh_terms: D019746:Intramolecular Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D012639:Seeds / Q000201:enzymology; D013379:Substrate Specificity; D003313:Zea mays / Q000201:enzymology*
chemical_list: D019746:Intramolecular Oxidoreductases; C021377:hydroperoxide isomerase