Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds.
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.
Utsunomiya
Y
Y
Faculty of Nutrition, Kobe Gakuin University, Hyogo, Japan.
Nakayama
T
T
Oohira
H
H
Hirota
R
R
Mori
T
T
Kawai
F
F
Ueda
T
T
D019746:Intramolecular Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D012639:Seeds / Q000201:enzymology; D013379:Substrate Specificity; D003313:Zea mays / Q000201:enzymology*
D019746:Intramolecular Oxidoreductases; C021377:hydroperoxide isomerase