Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds |
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| Authors: | Utsunomiya Y Nakayama T Oohira H Hirota R Mori T Kawai F Ueda T |
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| Affiliation: | Faculty of Nutrition, Kobe Gakuin University, Hyogo, Japan. |
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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. |
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