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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-12-4
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pubmed:abstractText |
The inhibition by m-coumaric acid of oxidation of L-dopa by epidermis tyrosinase (monophenol,dihydroxy-L-phenylalanine:oxygen oxidoreductase, EC 1.14.18.1) is characterized by a prolonged transient phase. Kinetic data correspond to that for a postulated mechanism that involves rapid formation of a reduced enzyme-m-coumaric acid complex that subsequently undergoes a relatively slow reversible reaction. An overall inhibition constant for m-coumaric acid of 0.05 mM was calculated. The value of the Ki for the dissociation of m-coumaric acid from the rapidly formed complex was calculated as 0.53 mM. The first-order rate constants for the slow isomerization of the enzyme-inhibitor complex were calculated as 3.0 +/- 0.1 min-1 for the forward step and 0.31 +/- 0.06 min-1 for the reverse step.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
790
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
101-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6435675-Animals,
pubmed-meshheading:6435675-Catechol Oxidase,
pubmed-meshheading:6435675-Cinnamates,
pubmed-meshheading:6435675-Coumaric Acids,
pubmed-meshheading:6435675-Kinetics,
pubmed-meshheading:6435675-Mathematics,
pubmed-meshheading:6435675-Models, Biological,
pubmed-meshheading:6435675-Monophenol Monooxygenase,
pubmed-meshheading:6435675-Rana esculenta,
pubmed-meshheading:6435675-Rana ridibunda,
pubmed-meshheading:6435675-Skin
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pubmed:year |
1984
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pubmed:articleTitle |
Kinetic study on the slow inhibition of epidermis tyrosinase by m-coumaric acid.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|