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Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase and Organism(s) Sus scrofa

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EC Tree
IUBMB Comments
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein .
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Word Map
The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipoamide dehydrogenase, dihydrolipoamide dehydrogenase, dldh, l-protein, dihydrolipoyl dehydrogenase, nadh diaphorase, e3 component, lipdh, nicotinamide adenine dinucleotide diaphorase, lipoyl dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, lipoamide
-
-
-
-
dehydrolipoate dehydrogenase
-
-
-
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DHLDH
-
-
-
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diaphorase
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoic dehydrogenase
-
-
-
-
dihydrolipoyl dehydrogenase
-
-
-
-
DLD
-
-
DT-diaphorase
-
-
E3
-
-
-
-
E3 component of 2-oxoglutarate dehydrogenase complex
-
-
-
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E3 component of acetoin cleaving system
-
-
-
-
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
-
-
-
-
E3 lipoamide dehydrogenase
-
-
-
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Glycine cleavage system L protein
-
-
-
-
Glycine oxidation system L-factor
-
-
-
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LAD
-
-
LDP-Glc
-
-
-
-
LDP-Val
-
-
-
-
LipDH
-
-
lipoamide dehydrogenase
lipoamide dehydrogenase (NADH)
-
-
-
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lipoamide oxidoreductase (NADH)
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-
-
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lipoamide reductase
-
-
-
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lipoate dehydrogenase
-
-
-
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lipoic acid dehydrogenase
-
-
-
-
lipoyl dehydrogenase
LPD
-
-
-
-
LPD-GLC
-
-
-
-
LPD-VAL
-
-
-
-
NAD(P)H:lipoamide oxidoreductase
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NADH diaphorase
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NADH:lipoamide oxidoreductase
-
-
-
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nicotinamide adenine dinucleotide diaphorase
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ORF-E3
-
-
-
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ubiquinone reductase
-
-
additional information
-
enzyme belongs to the family of pyridine nucleotide oxidoreductases
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
ping pong mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
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redox reaction
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-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-18-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
-
cytochrome c is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + NAD(P)H
3-aminotyrosine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
show the reaction diagram
-
-
-
-
?
8-nitroguanine + NAD(P)H
8-aminoguanine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + NAD(P)H
8-aminoxanthine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
acetaldoxime + NADH
?
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
?
DL-6,8-thiooctic acid amide + NADH
? + NAD+
show the reaction diagram
-
-
-
-
r
formaldoxime + NADH
?
show the reaction diagram
-
-
-
-
?
glycerol trinitrate + NADH
?
show the reaction diagram
-
-
-
-
?
hydroxylamine hydrochloride + NADH
?
show the reaction diagram
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
r
mature frataxin + NADH
denoted frataxin + NAD+
show the reaction diagram
-
exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity
-
-
?
metmyoglobin + NADH
reduced myoglobin + NAD+
show the reaction diagram
-
myoglobin is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
nitrated DNA + NAD(P)H
?
show the reaction diagram
-
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
-
-
?
nitric oxide + NADH
nitrate + NAD+
show the reaction diagram
-
-
-
-
?
O2 + NADH
H2O2 + NAD+
show the reaction diagram
oxidized lipoamide + NADH
reduced lipoamide + NAD+
show the reaction diagram
-
-
-
-
?
oxidized lipoic acid + NADH
reduced lipoic acid + NAD+
show the reaction diagram
-
-
-
-
?
S-nitroso-N-acetylpenicillamine + NADH
?
show the reaction diagram
-
-
-
-
?
S-nitrosoglutathione + NADH
?
show the reaction diagram
-
-
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-
?
sodium nitroprusside + NADH
?
show the reaction diagram
-
-
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-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nitrated DNA + NAD(P)H
?
show the reaction diagram
-
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
-
-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
show the reaction diagram
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dihydrolipoic acid
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-
NAD(P)H
ubiquinol
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-
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylene blue
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stimulates reduction of cytochrome c and myoglobin
Zn2+
-
stimulates the oxygen oxidase activity of the enzyme
additional information
-
activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation, Freezing–thawing results in further activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.45
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.96
acetaldoxime
-
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
-
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
-
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
-
dehydrogenase and oxidase activity kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
72 - 300
ubiquinone
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 0.8
diphenyleneiodonium chloride
additional information
additional information
-
Zn2+ inhibition kinetics and mechanism
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59 - 3.31
diphenyleneiodonium chloride
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
purified enzyme in absence of Zn2+
0.05
-
purified enzyme in presence of Zn2+
0.5
-
metmyoglobin reduction, in absence of methylene blue, pH 7.5
0.6
-
O2 reduction, pH 6.0
0.8
-
cytochrome c reduction, in absence of methylene blue, pH 7.5
1.7
-
lipoic acid reduction, pH 6.0
154
-
lipoamide reduction, pH 6.0
210
-
nitric oxide reduction, pH 6.0
4.5
-
metmyoglobin reduction, in presence of methylene blue, pH 7.5
6.4
-
cytochrome c reduction, in presence of methylene blue, pH 7.5
7.2
-
2,6-dichlorophenolindophenol reduction, pH 6.0
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
-
reduction of nitric oxide, lioamide, lipoic acid, and 2,6-dichlorophenolindophenol
5.5
-
optimum in absence of Zn2+
5.8
monomeric enzyme
6
-
optimum in presence of Zn2+
7
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
-
-
5 - 8
-
nitric oxide reduction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is part of multienzyme complexes in the inner mitochondrial membrane
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DLDH_PIG
509
0
54185
Swiss-Prot
Mitochondrion (Reliability: 2)
A0A8D2BS24_PIG
501
0
53296
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1HBV6_PIG
476
0
50719
TrEMBL
Mitochondrion (Reliability: 2)
A0A5G2QH34_PIG
511
0
54639
TrEMBL
Mitochondrion (Reliability: 2)
A0A4X1V436_PIG
486
0
51858
TrEMBL
Mitochondrion (Reliability: 2)
A0A5G2QGG6_PIG
486
0
51858
TrEMBL
Mitochondrion (Reliability: 2)
A0A4X1V5N5_PIG
509
0
54219
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D0JT66_PIG
510
0
54219
TrEMBL
Mitochondrion (Reliability: 5)
F1SAF0_PIG
509
0
54219
TrEMBL
Mitochondrion (Reliability: 2)
A0A480N1D9_PIG
476
0
50692
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D1WMS5_PIG
476
0
50692
TrEMBL
Mitochondrion (Reliability: 2)
A0A5G2QPK6_PIG
501
0
53296
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1KVU4_PIG
511
0
54639
TrEMBL
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
gel filtration
49690
-
x * 49690, calculation from nucleotide sequence
52000
2 * 52000, present at pH 5.8 and 7.5, active at pH 7.5
54000
1 * 54000, only present and active at pH 5.8
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
1 * 54000, only present and active at pH 5.8
tetramer
present at pH 5.8 and 7.5, active at pH 7.5
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by hanging-drop vapor-diffusion method
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on propyllipoamide-glass columns
-
further purification of the commercial preparation
-
further purification of the commercial preparation by gel filtration
-
partially
-
Sephadex G-25 column gel filtration
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
NADH diaphorase staining can establish tissue non-viability after radiofrequency ablation, but the timing of staining after treatment must be considered when interpreting results to avoid false positive tests. Tissue that is apparently viable by NADH diaphorase staining within 2.5 hours of radiofrequency ablation may in fact have been ablated
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Millard, S.A.; Kubose, A.; Gal, E.M.
Brain lipoyl dehydrogenase. Purification, properties, and inhibitors
J. Biol. Chem.
244
2511-2515
1969
Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Bjoernstedt, M.; Nordman, T.; Olsson, J.M.
Extramitochondrial reduction of ubiquinone by flavoenzymes
Methods Enzymol.
378
131-138
2004
Sus scrofa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team