Document Detail


Biosynthesis of Cutin omega-Hydroxylation of Fatty Acids by a Microsomal Preparation from Germinating Vicia faba.
MedLine Citation:
PMID:  16660004     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Abstract/OtherAbstract:
omega-Hydroxylation of fatty acids, which is a key reaction in the biosynthesis of cutin and suberin, has been demonstrated for the first time in a cell-free preparation from a higher plant. A crude microsomal fraction (105,000g pellet) from germinating embryonic shoots of Vicia faba catalyzed the conversion of palmitic acid to omega-hydroxypalmitic acid. As the crude cell-free preparation also catalyzes the formation of other hydroxy acids such as alpha- and beta-hydroxy acids, the omega-hydroxylation product was identified by gas chromatography on a polyester column and reverse phase, high performance liquid chromatography, two techniques which were shown to resolve the positional isomers. Gas chromatographic analysis of the dicarboxylic acid obtained by CrO(3) oxidation of the enzymic product also confirmed the identity of the enzymic omega-hydroxylation product. This enzymic hydroxylation required O(2) and NADPH, but substitution of NADH resulted in nearly half the reaction rate obtained with NADPH. Maximal rates of omega-hydroxylation occurred at pH 8 and the rate increased in a sigmoidal manner with increasing concentrations of palmitic acid. This omega-hydroxylation was inhibited by the classical mixed function oxidase inhibitors such as metal chelators (o-phenanthroline, 8-hydroxyquinoline, and alpha,alpha-dipyridyl), NaN(3) and thiol reagents (N-ethylmaleimide and p-chloromercuribenzoate). As expected of a hydroxylase, involving cytochrome P(450), the present omega-hydroxylase was inhibited by CO and this enzyme system showed unusually high sensitivity to this inhibition; 10% CO caused inhibition and 30% CO completely inhibited the reaction. Another unusual feature was that the inhibition caused by any level of CO could not be reversed by light (420-460 nm).
Authors:
C L Soliday; P E Kolattukudy
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Plant physiology     Volume:  59     ISSN:  0032-0889     ISO Abbreviation:  Plant Physiol.     Publication Date:  1977 Jun 
Date Detail:
Created Date:  2010-06-29     Completed Date:  2010-06-29     Revised Date:  2010-09-14    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1116-21     Citation Subset:  -    
Affiliation:
Department of Agricultural Chemistry and Program in Biochemistry and Biophysics, Washington State University, Pullman, Washington 99164.
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