rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
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pubmed:dateCreated |
1987-8-27
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pubmed:abstractText |
A microsomal preparation from the epidermis of Salvia officinalis leaves catalyzed the NADPH- and O2-dependent hydroxylation of the monoterpene olefin (+)-sabinene to (+)-cis-sabinol. The reaction catalyzed is a key step in the biosynthesis of C3-oxygenated thujane monoterpenes, and the hydroxylase is highly specific for (+)-sabinene as substrate. The hydroxylase from leaf homogenates was solubilized and characterized with regard to reaction conditions, inhibitors, and activators. Activity was partially inhibited by rabbit anti-rat cytochrome P-450 and by CO, and the latter inhibition was reversed by 450 nm light. A CO-difference spectrum and type I substrate binding spectrum were obtained. The hydroxylase meets most of the established criteria for a cytochrome P-450-dependent mixed function oxygenase and represents one of very few enzyme systems of this type to be isolated from leaves of a higher plant.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0003-9861
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
256
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
179-93
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3111374-Carbon Monoxide,
pubmed-meshheading:3111374-Cytochrome P-450 Enzyme System,
pubmed-meshheading:3111374-Hydroxylation,
pubmed-meshheading:3111374-Microsomes,
pubmed-meshheading:3111374-Mixed Function Oxygenases,
pubmed-meshheading:3111374-Monoterpenes,
pubmed-meshheading:3111374-NADPH-Ferrihemoprotein Reductase,
pubmed-meshheading:3111374-Phospholipids,
pubmed-meshheading:3111374-Plants,
pubmed-meshheading:3111374-Solubility,
pubmed-meshheading:3111374-Substrate Specificity,
pubmed-meshheading:3111374-Terpenes
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pubmed:year |
1987
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pubmed:articleTitle |
Metabolism of monoterpenes: demonstration of the hydroxylation of (+)-sabinene to (+)-cis-sabinol by an enzyme preparation from sage (Salvia officinalis) leaves.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|