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 |
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Pages (from-to) | 319-323 |
Number of pages | 5 |
Journal | Phytochemistry |
Volume | 53 |
Issue number | 3 |
DOIs | |
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