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

Authors
Utsunomiya, Y Nakayama, T Oohira, H Hirota, R Mori, T Kawai, F Ueda, T
Citation
Y. Utsunomiya et al., Purification and inactivation by substrate of an allene oxide synthase (CYP74) from corn (Zea mays L.) seeds, PHYTOCHEM, 53(3), 2000, pp. 319-323
Citations number
19
Categorie Soggetti
Agricultural Chemistry","Animal & Plant Sciences
Journal title
PHYTOCHEMISTRY
ISSN journal
00319422 → ACNP
Volume
53
Issue
3
Year of publication
2000
Pages
319 - 323
Database
ISI
SICI code
0031-9422(200002)53:3<319:PAIBSO>2.0.ZU;2-T
Abstract
The allene oxide synthase (AOS) was purified from corn (Zea mays) seeds to homogeneity and characterized partially. The corn AOS was a hemoprotein cyt ochrome 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. All rights reserved.