Pyridine Nucleotide — Disulfide Oxidoreductases
Pyridine Nucleotide — Disulfide Oxidoreductases
Electron transfer between pyridine nucleotides and disulfide compounds is catalyzed by three flavoproteins which are well characterized. Lipoamide dehydrogenase reoxidizes reduced lipoamide (lip-(SH)2) by NAD+. Glutathione reductase catalyzes reduction of glutathione (GSSG) by NADPH. Thioredoxin reductase catalyzes the reduction of oxidized thioredoxin (thioredoxin-S2) by NADPH. These three enzymes resemble each other structurally and mechanistically. They have, in addition to FAD, a redox active disulfide which is functional in catalysis. The flavoproteins consist of two identical or near identical polypeptide chains, each with a functional cystine residue, and a molecule of FAD which is noncovalently linked.
Models, Molecular, Binding Sites, Thioredoxin-Disulfide Reductase, Macromolecular Substances, Protein Conformation, NAD, Glutathione Reductase, Multienzyme Complexes, Escherichia coli, Flavin-Adenine Dinucleotide, Animals, NADH, NADPH Oxidoreductases, Amino Acid Sequence, Disulfides, NADP, Dihydrolipoamide Dehydrogenase
Models, Molecular, Binding Sites, Thioredoxin-Disulfide Reductase, Macromolecular Substances, Protein Conformation, NAD, Glutathione Reductase, Multienzyme Complexes, Escherichia coli, Flavin-Adenine Dinucleotide, Animals, NADH, NADPH Oxidoreductases, Amino Acid Sequence, Disulfides, NADP, Dihydrolipoamide Dehydrogenase
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