rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1984-7-20
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pubmed:abstractText |
Guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of (Rp)-guanosine 5'-(3-thio[3-18O]triphosphate) and oxalacetate to (Sp)-[18O] thiophosphoenolpyruvate , GDP, and CO2 by a mechanism that involves overall inversion in the configuration of the chiral [18O]thiophosphate group. This result is most consistent with a single displacement mechanism in which the [18O]thiophosphoryl group is transferred from (Rp)-guanosine 5'-(3-thio[3-18O]triphosphate) bound at the active site directly to enolpyruvate generated at the active site by the decarboxylation of oxalacetate. In particular, this result does not indicate the involvement of a covalent thiophosphoryl-enzyme on the reaction pathway.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-2960
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1779-83
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6372862-Animals,
pubmed-meshheading:6372862-Binding Sites,
pubmed-meshheading:6372862-Chromatography, Gas,
pubmed-meshheading:6372862-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:6372862-Guanosine Triphosphate,
pubmed-meshheading:6372862-Guinea Pigs,
pubmed-meshheading:6372862-Kinetics,
pubmed-meshheading:6372862-Mitochondria, Liver,
pubmed-meshheading:6372862-Oxaloacetates,
pubmed-meshheading:6372862-Oxaloacetic Acids,
pubmed-meshheading:6372862-Oxygen Isotopes,
pubmed-meshheading:6372862-Phosphoenolpyruvate,
pubmed-meshheading:6372862-Phosphoenolpyruvate Carboxykinase (GTP),
pubmed-meshheading:6372862-Protein Binding,
pubmed-meshheading:6372862-Thionucleotides
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pubmed:year |
1984
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pubmed:articleTitle |
Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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