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dehydrogenase, lipoamide
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dehydrolipoate dehydrogenase
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dihydrolipoamide dehydrogenase
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dihydrolipoamide dehydrogenase E3
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common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoic dehydrogenase
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dihydrolipoyl dehydrogenase
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E3 component of 2-oxoglutarate dehydrogenase complex
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E3 component of acetoin cleaving system
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E3 component of alpha keto acid dehydrogenase complexes
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E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
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E3 component of pyruvate complex
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E3 lipoamide dehydrogenase
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Glycine cleavage system L protein
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Glycine oxidation system L-factor
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lipoamide dehydrogenase (NADH)
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lipoamide oxidoreductase (NADH)
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lipoamide reductase
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lipoate dehydrogenase
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lipoic acid dehydrogenase
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NAD(P)H:lipoamide oxidoreductase
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NADH:lipoamide oxidoreductase
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nicotinamide adenine dinucleotide diaphorase
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additional information
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enzyme belongs to the family of pyridine nucleotide oxidoreductases
diaphorase
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DLDH
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LADH
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoyl dehydrogenase
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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
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?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
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cytochrome c is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
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?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
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?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
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?
3-nitrotyrosine + NAD(P)H
3-aminotyrosine + NAD(P)+ + H2O
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?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
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?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
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?
8-nitroguanine + NAD(P)H
8-aminoguanine + NAD(P)+ + H2O
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?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
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?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
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?
8-nitroxanthine + NAD(P)H
8-aminoxanthine + NAD(P)+ + H2O
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?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
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?
acetaldoxime + NADH
?
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?
dihydrolipoamide + NAD+
lipoamide + NADH
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?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
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?
DL-6,8-thiooctic acid amide + NADH
? + NAD+
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r
formaldoxime + NADH
?
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?
glycerol trinitrate + NADH
?
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?
hydroxylamine hydrochloride + NADH
?
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?
lipoamide + NADH
dihydrolipoamide + NAD+
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r
mature frataxin + NADH
denoted frataxin + NAD+
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exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity
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?
metmyoglobin + NADH
reduced myoglobin + NAD+
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myoglobin is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
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?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
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?
nitrated DNA + NAD(P)H
?
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enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination which can cause cancer, enzyme might be resonsible for reversing biological nitration processes
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?
nitric oxide + NADH
nitrate + NAD+
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?
oxidized lipoamide + NADH
reduced lipoamide + NAD+
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?
oxidized lipoic acid + NADH
reduced lipoic acid + NAD+
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?
S-nitroso-N-acetylpenicillamine + NADH
?
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?
S-nitrosoglutathione + NADH
?
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?
sodium nitroprusside + NADH
?
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?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
additional information
?
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O2 + NADH
H2O2 + NAD+
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?
O2 + NADH
H2O2 + NAD+
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the enzyme produces reactive oxygen species, i.e. hydrogen peroxide, acting as an oxidase
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?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
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?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
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ir
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
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enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
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?
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
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?
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
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reaction is important to protect the cell e.g. from oxidative stress
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?
additional information
?
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substrate specificity, overview
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?
additional information
?
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diaphorase activity
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?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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?
additional information
?
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the enzyme might play a role in modifying NO levels under specific cell conditions
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?
additional information
?
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LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
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?
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2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine hydrochloride
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inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
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inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-amino-4-hydroxy-6-methyl-7,8-dihydropteridine
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inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
diisopropyl fluorophosphate
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DLD is fully inactivated by 1 mM
diphenyleneiodonium chloride
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folic acid
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inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
isobiopterin
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inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
N-ethylmaleimide
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over 90% inhibition at 1 mM
NAD(P)+
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product inhibition
NAD+
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product inhibition of the oxygen oxidase activity
Zn2+
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reversible binding, competitive to lipoamide, uncompetitive to NADH
additional information
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no inhibition of the nitric oxide reduction by cyanide, antimycin A, or diphenyleneiodonium ions
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additional information
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LAD is not inhibited by resorufin ethyl ether, phenidone, Nomega-nitro-L-arginine methyl ester hydrochloride, proadiphen hydrochloride, and miconazole nitrate
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1.45
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.96
acetaldoxime
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.73 - 17.18
formaldoxime
0.9 - 2.27
glycerol trinitrate
3.24
Hydroxylamine hydrochloride
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.01
NADH
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nitric oxide reduction, pH 7.5
0.0005
NO
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nitric oxide reduction, pH 7.5
0.42 - 5.48
S-nitroso-N-acetylpenicillamine
0.12 - 0.44
S-nitrosoglutathione
0.84 - 2.26
sodium nitroprusside
additional information
additional information
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dehydrogenase and oxidase activity kinetics
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2.73
formaldoxime
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
17.18
formaldoxime
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.9
glycerol trinitrate
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.27
glycerol trinitrate
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.42
S-nitroso-N-acetylpenicillamine
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
5.48
S-nitroso-N-acetylpenicillamine
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.12
S-nitrosoglutathione
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.44
S-nitrosoglutathione
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.84
sodium nitroprusside
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in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.26
sodium nitroprusside
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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0.29 - 0.8
diphenyleneiodonium chloride
additional information
additional information
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Zn2+ inhibition kinetics and mechanism
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0.29
diphenyleneiodonium chloride
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using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.31
diphenyleneiodonium chloride
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using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.35
diphenyleneiodonium chloride
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using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.45
diphenyleneiodonium chloride
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using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.56
diphenyleneiodonium chloride
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using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.6
diphenyleneiodonium chloride
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using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.8
diphenyleneiodonium chloride
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using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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0.59 - 3.31
diphenyleneiodonium chloride
0.59
diphenyleneiodonium chloride
Sus scrofa
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using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.68
diphenyleneiodonium chloride
Sus scrofa
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.75
diphenyleneiodonium chloride
Sus scrofa
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.81
diphenyleneiodonium chloride
Sus scrofa
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.93
diphenyleneiodonium chloride
Sus scrofa
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.61
diphenyleneiodonium chloride
Sus scrofa
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
3.31
diphenyleneiodonium chloride
Sus scrofa
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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Toyoda, T.; Kobayashi, R.; Sekiguchi, T.; Koike, K.; Koike, M.; Takenaka, A.
Crystallization and preliminary X-ray analysis of pig E3, lipoamide dehydrogenase
Acta Crystallogr. Sect. D
54
982-985
1998
Peptoclostridium acidaminophilum, Sus scrofa
brenda
Carothers, D.J.; Pons, G.; Patel, M.S.
Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases
Arch. Biochem. Biophys.
268
409-425
1989
Ascaris suum, Azotobacter vinelandii, Bacillus subtilis, Bos taurus, Escherichia coli, Geobacillus stearothermophilus, Halobacterium salinarum, Homo sapiens, Pisum sativum, Pseudomonas aeruginosa, Pseudomonas putida, Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces pastorianus, Sus scrofa
brenda
Tsai, C.S.; Wand, A.J.; Templeton, D.M.; Weiss, P.M.
Multifunctionality of lipoamide dehydrogenase promotion of electron transferase reaction
Arch. Biochem. Biophys.
225
554-561
1983
Sus scrofa
brenda
Williams, C.H.
Flavin-containing dehydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
89-173
1976
Azotobacter agilis, Azotobacter vinelandii, Bacillus subtilis, Bos taurus, Brassica oleracea, Enterococcus faecalis, Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli Crookes, Escherichia coli M191-6, Globisporangium ultimum, Homo sapiens, Leuconostoc mesenteroides, Mycobacterium tuberculosis, Neurospora crassa, Parvimonas micra, Phytophthora erythroseptica, Pichia kudriavzevii, Proteus vulgaris, Pseudomonas fluorescens, Rattus norvegicus, Saccharomyces cerevisiae, Serratia marcescens, Spinacia oleracea, Squalus acanthias, Sus scrofa
-
brenda
Scouten, W.H.; Torok, F.; Gitomer, W.
Purification of lipoamide dehydrogenase by affinity chromatography on propyllipoamide-glass columns
Biochim. Biophys. Acta
309
521-524
1973
Saccharomyces cerevisiae, Sus scrofa
brenda
Millard, S.A.; Kubose, A.; Gal, E.M.
Brain lipoyl dehydrogenase. Purification, properties, and inhibitors
J. Biol. Chem.
244
2511-2515
1969
Sus scrofa
brenda
Nordman, T.; Xia, L.; Bjorkhem-Bergman, L.; Damdimopoulos, A.; Nalvarte, I.; Arner, E.S.; Spyrou, G.; Eriksson, L.C.; Bjornstedt, M.; Olsson, J.M.
Regeneration of the antioxidant ubiquinol by lipoamide dehydrogenase, thioredoxin reductase and glutathione reductase
Biofactors
18
45-50
2003
Sus scrofa
brenda
Chen, H.J.; Chen, Y.M.; Chang, C.M.
Lipoyl dehydrogenase catalyzes reduction of nitrated DNA and protein adducts using dihydrolipoic acid or ubiquinol as the cofactor
Chem. Biol. Interact.
140
199-213
2002
Clostridium kluyveri, Sus scrofa
brenda
Xia, L.; Bjrnstedt, M.; Nordman, T.; Eriksson, L.C.; Olsson, J.M.
Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway
Eur. J. Biochem.
268
1486-1490
2001
Sus scrofa
brenda
Igamberdiev, A.U.; Bykova, N.V.; Ens, W.; Hill, R.D.
Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide
FEBS Lett.
568
146-150
2004
Sus scrofa
brenda
Gazaryan, I.G.; Krasnikov, B.F.; Ashby, G.A.; Thorneley, R.N.; Kristal, B.S.; Brown, A.M.
Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
J. Biol. Chem.
277
10064-10072
2002
Sus scrofa
brenda
Bjoernstedt, M.; Nordman, T.; Olsson, J.M.
Extramitochondrial reduction of ubiquinone by flavoenzymes
Methods Enzymol.
378
131-138
2004
Sus scrofa
brenda
Klyachko, N.L.; Shchedrina, V.A.; Efimov, A.V.; Kazakov, S.V.; Gazaryan, I.G.; Kristal, B.S.; Brown, A.M.
pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification
J. Biol. Chem.
280
16106-16114
2005
Sus scrofa (P09623), Sus scrofa
brenda
Anderson, J.K.; Baker, M.; Jaffers, O.; Pearle, M.S.; Lindberg, G.L.; Cadeddu, J.A.
Time course of nicotinamide adenine dinucleotide diaphorase staining after renal radiofrequency ablation influences viability assessment
J. Endourol.
21
223-227
2007
Sus scrofa
brenda
Babady, N.E.; Pang, Y.P.; Elpeleg, O.; Isaya, G.
Cryptic proteolytic activity of dihydrolipoamide dehydrogenase
Proc. Natl. Acad. Sci. USA
104
6158-6163
2007
Homo sapiens, Mus musculus, Sus scrofa
brenda
Stibingerova, A.; Velvarska, H.; Kynclova, K.; Marounkova, B.; Spundova, M.; Entlicher, G.
Lipoamide dehydrogenase and diaphorase catalyzed conversion of some NO donors to NO and reduction of NO scavenger 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO)
Gen. Physiol. Biophys.
28
384-390
2009
Bos taurus, Sus scrofa
brenda