PROPERTIES AND STRUCTURES OF FATTY-ACID HYDROPEROXIDE LYASE

Authors
Citation
K. Matsui, PROPERTIES AND STRUCTURES OF FATTY-ACID HYDROPEROXIDE LYASE, Belgian journal of botany, 131(1), 1998, pp. 50-62
Citations number
68
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
07784031
Volume
131
Issue
1
Year of publication
1998
Pages
50 - 62
Database
ISI
SICI code
0778-4031(1998)131:1<50:PASOFH>2.0.ZU;2-B
Abstract
Fatty acid hydroperoxide lyase (HPOL) is an enzyme that cleaves fatty acid hydroperoxides to form a short chain aldehyde and an oxo-acid. Th e enzyme is widely distributed in the plant kingdom. Because short cha in aldehydes have fungicidal activity and can act as repellents of cer tain insects and attractants for insect predators, HPOL is thought to be involved in plant defense mechanisms. Recently, HPOL has been purif ied from several plants and its biochemical properties determined. Fur thermore, molecular cloning of an HPOL gene from bell pepper has been accomplished. Determination of the primary amino acid sequence showed that HPOL defines a novel subfamily of cytochrome P450s.