Document Detail

Inactivation of alcohol dehydrogenase in rice seedlings is related to a microsomal fatty acid alpha-oxidation system.
MedLine Citation:
PMID:  2939066     Owner:  NLM     Status:  MEDLINE    
The selective inactivation of alcohol dehydrogenase by the inactivator found in the microsomal fraction of rice (Oryza sativa) seedlings growing in air (Shimomura, S. & Beevers, H. (1983) Plant Physiol. 71, 736-741; 742-746) was further studied. This inactivation was found to be essentially dependent on the presence of free fatty acids. The specificity for fatty acids and the inhibitory effects of imidazole, 2-hydroxyfatty acids and dithiothreitol on the inactivation were all consistent with the properties of the fatty acid alpha-oxidation system in plants. Both O2 consumption and decarboxylation of fatty acid due to alpha-oxidation were also demonstrated in rice microsomes. When purified rice alcohol dehydrogenase was added to the alpha-oxidation system in rice microsomes, the decarboxylation of fatty acid was inhibited, and the cysteinyl residues of alcohol dehydrogenase were oxidized. The oxidation of two cysteinyl residues per monomer resulted in the complete inactivation of the enzyme. The activity of the inactivator in the isolated microsomes was gradually lost during storage and was rapidly lost upon heating. The inactivation of alcohol dehydrogenase was observed even when the enzyme was separated from microsomes by a dialysis membrane. These results indicate that the inactivation of alcohol dehydrogenase is closely related to fatty acid alpha-oxidation. We postulate that an intermediate of alpha-oxidation is the inactivator.
M Y Kang; S Shimomura; T Fukui
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  99     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1986 Feb 
Date Detail:
Created Date:  1986-06-09     Completed Date:  1986-06-09     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  549-59     Citation Subset:  IM    
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MeSH Terms
Alcohol Dehydrogenase
Alcohol Oxidoreductases / antagonists & inhibitors*
Fatty Acids / metabolism*,  pharmacology
Microsomes / metabolism
Oryza sativa / metabolism
Oxygen Consumption
Peroxides / pharmacology
Plants / metabolism*
Sulfhydryl Compounds / metabolism
Reg. No./Substance:
0/Fatty Acids; 0/Peroxides; 0/Sulfhydryl Compounds; EC 1.1.-/Alcohol Oxidoreductases; EC Dehydrogenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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