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pubmed-article:15535970pubmed:dateCreated2004-11-10lld:pubmed
pubmed-article:15535970pubmed:abstractTextDelta1-pyrroline-5-carboxylate dehydrogenase (P5CDh) catalyzes the conversion of Delta1-pyrroline-5-carboxylate to glutamate in a reaction requiring NADP+ as a cofactor. Delta1-pyrroline-5-carboxylate is formed in liver from proline by proline oxidase (EC number not assigned) or from ornithine via ornithine aminotransferase. A spectrophotometric assay for P5CDh was shown to be valid if rotenone was included in the assay to prevent reoxidation of NADH. Using this new assay, liver was fractionated using differential centrifugation and the distribution of P5CDh was compared to that of appropriate marker enzymes. P5CDh is enriched only in the mitochondrial fractions, as are the mitochondrial enzymes, succinate cytochrome c reductase, proline oxidase, glutaminase, and ornithine aminotransferase. Thus, it can be concluded that P5CDh occurs only in mitochondria, not in both mitochondria and cytoplasm, as had previously been reported.lld:pubmed
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pubmed-article:15535970pubmed:pagination81-6lld:pubmed
pubmed-article:15535970pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15535970pubmed:year2004lld:pubmed
pubmed-article:15535970pubmed:articleTitleAssay and subcellular localization of pyrroline-5-carboxylate dehydrogenase in rat liver.lld:pubmed
pubmed-article:15535970pubmed:affiliationDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, NF Canada A1B 3X9.lld:pubmed
pubmed-article:15535970pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15535970pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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