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DIHYDROLIPOAMIDE DEHYDROGENASE

Known as: Diaphorase, NAD, Dehydrogenase, Lipoic Acid, Lipoyl Dehydrogenase 
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a… Expand
National Institutes of Health

Related topics

Related topics

10 relations
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects
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Broader (1)

respiratory enzyme

Papers overview

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Review
2007
Review
2007
Cyanobacterial hydrogenases: diversity, regulation and applications.
Cyanobacteria may possess two distinct nickel-iron (NiFe)-hydrogenases: an uptake enzyme found in N(2)-fixing strains, and a… Expand
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Highly Cited
2004
Highly Cited
2004
Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species.
Mitochondria-produced reactive oxygen species (ROS) are thought to contribute to cell death caused by a multitude of pathological… Expand
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Highly Cited
2002
Highly Cited
2002
Two-photon fluorescence spectroscopy and microscopy of NAD(P)H and flavoprotein.
Two-photon (2P) ratiometric redox fluorometry and microscopy of pyridine nucleotide (NAD(P)H) and flavoprotein (FP) fluorescence… Expand
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Highly Cited
1998
Highly Cited
1998
A methanol/dioxygen biofuel cell that uses NAD+-dependent dehydrogenases as catalysts: application of an electro-enzymatic method to regenerate nicotinamide adenine dinucleotide at low overpotentials
Abstract Diaphorase catalyzes efficiently the oxidation of NADH to NAD + by benzylviologen. This reaction was used to regenerate… Expand
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Highly Cited
1992
Highly Cited
1992
NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity.
NAD(P)H:quinone oxidoreductase (DT-diaphorase; DTD) is an obligate two-electron reductase which may play a role in the… Expand
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Highly Cited
1979
Highly Cited
1979
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.
  • A. Holmgren
  • The Journal of biological chemistry
  • 1979
    • Corpus ID: 11371465
Thioredoxin from Escherichia coli was shown to catalyze the reduction of insulin disulfides by dithiothreitol. A quantitative… Expand
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Highly Cited
1976
Highly Cited
1976
Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16.
The soluble hydrogenase (hydrogen: NAD+ oxidoreductase, EC 1.12.1.2) from Alcaligenes eutrophus H 16 was purified 68-fold with a… Expand
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Highly Cited
1968
Highly Cited
1968
ENZYMATIC PROPERTIES OF THE INNER AND OUTER MEMBRANES OF RAT LIVER MITOCHONDRIA
Treatment of rat liver mitochondria with digitonin followed by differential centrifugation was used to resolve the… Expand
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Highly Cited
1965
Highly Cited
1965
On the reaction mechanism of yeast glutathione reductase.
Glutathione reductase has been purified from a number of sources, Escherichiu coli (l), yeast (2, 3), peas (4), rat tissues (5, 6… Expand
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Highly Cited
1958
Highly Cited
1958
A Histochemical Method for the Demonstration of Diphosphopyridine Nucleotide Diaphorase
The present investigation concerning the histochemical demonstration of DPN diaphorase follows the development of a new reagent… Expand
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