Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q8NEX9 (reductase)
 26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Incubation of malic enzyme (L-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating), EC 1.1.1.40) with ethoxyformic anhydride caused the time-dependent loss of its ability to catalyze reactions requiring the nucleotide cofactor NADP+ or NADPH, such as the oxidative decarboxylase, the NADP+ - stimualted oxalacetate decarboxylase, the pyruvate reductase, and the pyruvate-medium proton exchange activities. Similar loss of oxidative decarboxylase and pyruvate reductase activities was affected by photo-oxidation in the presence of rose bengal. The inactivation of oxidative decarboxylase activity by ethoxyformic anhydride was accompanied by the reaction of greater than or equal to 2.3 histidyl residues per enzyme site and was strongly inhibited by NADP+. Ethoxyformylation also impaired the ability of malic enzyme to bind NADP+ or NADPH. These results support the involvement of histidyl residue(s) at the nucleotide binding site of malic enzyme.
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PMID:Mechanism of pigeon liver malic enzyme modification of histidyl residues by ethoxyformic anhydride. 1 63

The nucleotide sequence of the mRNA for malic enzyme ((S)-malate NADP+ oxidoreductase (oxaloacetate-decarboxylating, EC 1.1.1.40) from rat liver was determined from three overlapping cDNA clones. Together, these clones contain 2078 nucleotides complementary to rat liver malic enzyme mRNA. The single open reading frame of 1761 nucleotides codes for a 585-amino acid polypeptide with a calculated molecular mass of about 65,460 daltons. The cloned cDNAs contain the complete 3'-noncoding region of 301 nucleotides for the major mRNA species of rat liver and 16 nucleotides of the 5'-noncoding region. Amino acid sequences of seven tryptic peptides (67 amino acids) from the purified protein are distributed through the single open reading frame and show excellent correspondence with the translated nucleotide sequence. The putative NADP-binding site for malic enzyme was identified by amino acid sequence homology with the NADP-binding site of the enoyl reductase domain of fatty acid synthetase.
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PMID:Coding nucleotide sequence of rat liver malic enzyme mRNA. 375 99

Nitric oxide (NO) and hydrogen sulfide (H2S) are two key molecules in plant cells which participate, directly or indirectly, as regulators of protein functions through derived posttranslational modifications (PTMs) mainly tyrosine nitration, S-nitrosation and persulfidation. These PTMs allow the participation of both NO and H2S signal molecules in a wide range of cellular processes either physiological or under stressful circumstances. NADPH partakes in the cellular redox status and it is a key cofactor necessary for cell growth and development because it participates in significant biochemical routes such as fatty acid, carotenoid and proline biosynthesis, shikimate pathway as well as in cellular detoxification processes including the ascorbate-glutathione cycle, the NADPH-dependent thioredoxin reductase (NTR) or the superoxide-generating NADPH oxidase. Plant cells have diverse mechanism to generate NADPH by a group of NADP-dependent oxidoreductases including the ferredoxin-NADP reductase (FNR), NADP-glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH), NADP-dependent malic enzyme (NADP-ME), NADP-dependent isocitrate dehydrogenase (NADP-ICDH), and both enzymes of the oxidative pentose phosphate pathway (OxPPP), designated as glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH). These enzymes consist of different isozymes located in diverse subcellular compartments (chloroplasts, cytosol, mitochondria and peroxisomes) which contribute to the NAPDH cellular pool. The present review provides a comprehensive overview about how PTMs promoted by NO (Tyr-nitration and S-nitrosation), H2S (persulfidation) and glutathione (glutathionylation), affect the cellular redox status through the regulation of the NADP-dependent dehydrogenases.
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PMID:Nitric oxide (NO) and hydrogen sulfide (H2S) modulate the NADPH-generating enzymatic system in higher plants. 3294 78