Name | pyridine nucleotide transhydrogenase |
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Synonyms | NNT; NNT protein; Nicotinamide nucleotide transhydrogenase; Pyridine nucleotide transhydrogenase; NNT proteins; Nicotinamide nucleotide transhydrogenases; Pyridine nucleotide transhydrogenases |
Name | rotenone |
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CAS |
PubMed | Abstract | RScore(About this table) | |
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1403417 | Fioravanti CF, McKelvey JR, Reisig JM: Energy-linked mitochondrial pyridine nucleotide transhydrogenase of adult Hymenolepis diminuta. J Parasitol. 1992 Oct;78(5):774-8. The isolated particles displayed rotenone-sensitive utilization and the reversible transhydrogenase, with the ----NAD+ transhydrogenation being more prominent. |
2(0,0,0,2) | Details |
4395037 | Rydstrom J, da Cruz AT, Ernster L: Factors governing the kinetics and steady state of the mitochondrial nicotinamide nucleotide transhydrogenase system. Eur J Biochem. 1970 Nov;17(1):56-62. |
1(0,0,0,1) | Details |
549647 | Klimek J, Boguslawski W, Zelewski L: The relationship between energy generation and cleavage reaction in the mitochondria from human term placenta. Biochim Biophys Acta. 1979 Oct 18;587(3):362-72. ADP and ATP stimulated the and alpha-ketoglutarate-supported biosynthesis probably via the energy-dependent pyridine nucleotide transhydrogenase activation. The effect of ADP was abolished by rotenone and antimycin in the presence of or alpha-ketoglutarate. 3. |
side-chain 1(0,0,0,1) | Details |
1757194 | Goyal N, Gupta S, Katiyar JC, Srivastava VM: The membranes also exhibited the presence of a reduced pyridine nucleotide transhydrogenase activity which transferred from to Amongst respiratory inhibitors, rotenone (Site I inhibitor) markedly depressed both oxidase and reductase while others, namely antimycin-A, KCN and azide, had a lesser effect. |
oxidase and reductase of Ancylostoma ceylanicum. Int J Parasitol. 1991 Oct;21(6):673-6.1(0,0,0,1) | Details |
2267725 | Goyal N, Srivastava VM: Mitochondrial The membrane preparation also exhibited the presence of a reduced pyridine nucleotide transhydrogenase which converted into by transferring a hydride ion. The oxidase activity was inhibited by all the respiratory inhibitors examined, with the greatest sensitivity to rotenone, a site I-specific inhibitor. |
oxidase activity of Setaria cervi. Vet Parasitol. 1990 Nov;37(3-4):229-36.1(0,0,0,1) | Details |