Abstract
It had been noted previously that the activity of mitochondrial dihydroorotate dehydrogenase was lower in crude tissue preparations containing cytosol than in isolated mitochondria. Closer examination reveals that the apparent lower enzyme activity is due to rapid conversion of newly-synthesized orotate to uridine-5-monophosphate by the cytosolic enzymes, orotate phosphoribosyltransferase and orotidylate decarboxylase.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Carboxy-Lyases / metabolism*
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Cytosol / enzymology*
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Dihydroorotate Oxidase / metabolism
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Liver / enzymology*
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Male
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Mitochondria, Liver / enzymology
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Orotate Phosphoribosyltransferase / metabolism*
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Orotic Acid / metabolism*
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Orotidine-5'-Phosphate Decarboxylase / metabolism*
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Pentosyltransferases / metabolism*
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Phosphoribosyl Pyrophosphate / metabolism
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Rats
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Rats, Inbred Strains
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Uracil Nucleotides / metabolism*
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Uridine Monophosphate / metabolism*
Substances
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Uracil Nucleotides
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Orotic Acid
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Phosphoribosyl Pyrophosphate
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Uridine Monophosphate
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Dihydroorotate Oxidase
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Pentosyltransferases
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Orotate Phosphoribosyltransferase
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Carboxy-Lyases
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Orotidine-5'-Phosphate Decarboxylase