Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
about
Glutathione reductase from germinated peasThe mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coliFunctional Role for the Conformationally Mobile Phenylalanine 223 in the Reaction of Methylenetetrahydrofolate Reductase from Escherichia coliTriazaspirodimethoxybenzoyls as Selective Inhibitors of Mycobacterial Lipoamide Dehydrogenase,Changes in dihydrolipoamide dehydrogenase expression and activity during postnatal development and aging in the rat brainConformational studies on lipoamide dehydrogenase from pig heart. I. Interconversion of dissociable and non-dissociable forms.A pH-dependent kinetic model of dihydrolipoamide dehydrogenase from multiple organisms.Radical mechanisms for 1,5-dihydroflavin reduction of carbonyl compounds.Leigh's subacute necrotizing encephalopathy: clinical and biochemical study, with special reference to therapy with lipoate.Isolation of a specific lipoamide dehydrogenase for a branched-chain keto acid dehydrogenase from Pseudomonas putidaMetabolism in infection: study on the enzymatic damage in kidney of guinea pig infected with Mycobacterium tuberculosisReversible inactivation of dihydrolipoamide dehydrogenase by Angeli's salt.Global Kinetic Analysis of Mammalian E3 Reveals pH-dependent NAD+/NADH Regulation, Physiological Kinetic Reversibility, and Catalytic OptimumSerum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.Human augmenter of liver regeneration: probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase.Glutathione reductase from human erythrocytes. Molecular weight, subunit composition and aggregation properties.S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.Enzymatic behaviour of lipoamide dehydrogenase isoenzymes immobilized on N-alkyl sepharose matrices.Flavin-nicotinamide biscoenzymes: models for the interaction between NADH (NADPH) and flavin in flavoenzymes. Reaction rates and physicochemical properties of intermediate species.An amino acid sequence in the active site of lipoamide dehydrogenase from pig heart.Effects of inhibitors on mitochondrial D-alpha-hydroxy acid dehydrogenase.The nature of compounds present in mixtures of oxidized and reduced flavin mononucleotides.Adenosine triphosphate-nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei. Extraction and purification of the enzyme.The reaction of choline dehydrogenase with some electron acceptors.The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase.Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds.Kinetic studies of liver alcohol dehydrogenase.The kinetic behaviour of enzymes in organized systems. Mitochondrial succinate oxidase and fumarase.Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase.Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species.The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster.Amino acid composition of thioredoxin reductase from Escherichia coli B.Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE.Intrinsic luminescence studies on the apoenzyme and holoenzyme of lipoamide dehydrogenase.An amino acid sequence in the active site of lipoamide dehydrogenase from the 2-oxoglutarate dehydrogenase complex of E. coli (Crookes strain).Spectroscopic studies of the characterization of recombinant human dihydrolipoamide dehydrogenase and its site-directed mutants.Stimulation of reactive oxygen species generation by disease-causing mutations of lipoamide dehydrogenaseEnzymatic Characterization of Dihydrolipoamide Dehydrogenase fromStreptococcus pneumoniaeHarboring Its Own Substrate
P2860
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P2860
Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
description
1960 nî lūn-bûn
@nan
1960年の論文
@ja
1960年論文
@yue
1960年論文
@zh-hant
1960年論文
@zh-hk
1960年論文
@zh-mo
1960年論文
@zh-tw
1960年论文
@wuu
1960年论文
@zh
1960年论文
@zh-cn
name
Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
@en
Intermediates in the catalytic action of lipoyl dehydrogenase
@nl
type
label
Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
@en
Intermediates in the catalytic action of lipoyl dehydrogenase
@nl
prefLabel
Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
@en
Intermediates in the catalytic action of lipoyl dehydrogenase
@nl
P2093
P2860
P356
P1433
P1476
Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
@en
P2093
P2860
P304
P356
10.1042/BJ0770341
P407
P577
1960-11-01T00:00:00Z