Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phosphate-activated glutaminase (PAG) mediating the conversion of glutamine to glutamate and ammonia, appears to be the major glutamate metabolizing enzyme in brain. The functional relevance of PAG in postnatally maturing glutamatergic/aspartatergic structures of the rat hippocampus was studied by means of quantitative enzyme histochemistry as an alternative to immunocytochemical techniques. The calibration of the histochemical PAG reaction as well as several control experiments for specificity were carried out to ensure reliability of findings. PAG activity increased markedly during the first weeks of life with a drastic rise between postnatal days 12 and 15. On the other hand, activity of NADH diaphorase involved in the histochemical PAG assay as an auxiliary enzyme, showed a different distribution pattern as well as a different developmental sequence with high levels early in ontogenesis. The topographical and temporal parallelisms of PAG activity to several other parameters which are putatively associated with postnatally maturing glutamatergic/aspartatergic transmission processes, mutually indicate their significance in such a functional context.
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PMID:Histochemically demonstrable activity of phosphate-activated glutaminase in the postnatally developing rat hippocampus. 340 93

Delta1-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.
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PMID:Assay and subcellular localization of pyrroline-5-carboxylate dehydrogenase in rat liver. 1553 70