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coronin-interacting protein
dehydrogenase, lipoamide
-
-
-
-
dehydrolipoate dehydrogenase
-
-
-
-
dihydrolipoamide dehydrogenase
dihydrolipoamide dehydrogenase E3
dihydrolipoamide:NAD+ oxidoreductase
dihydrolipoic dehydrogenase
-
-
-
-
dihydrolipomide dehydrogenase
-
dihydrolipoyl dehydrogenase
-
-
-
-
E3 component of 2-oxoglutarate dehydrogenase complex
-
-
-
-
E3 component of acetoin cleaving system
-
-
-
-
E3 component of alpha keto acid dehydrogenase complexes
-
-
-
-
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
-
-
-
-
E3 component of pyruvate complex
-
-
-
-
E3 lipoamide dehydrogenase
-
-
-
-
E3 protein component of 2-oxoacid dehydrogenase multienzyme complexes
-
-
E3 subunit of the alpha-ketoglutarate dehydrogenase complex
-
EC 1.6.4.3
-
-
formerly
-
Glycine cleavage system L protein
-
-
-
-
Glycine oxidation system L-factor
-
-
-
-
lipoamide dehydrogenase (NADH)
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-
-
-
lipoamide dehydrogenase C
lipoamide dehydrogenase2
-
lipoamide oxidoreductase (NADH)
-
-
-
-
lipoamide reductase
-
-
-
-
lipoamide-dehydrogenase-valine
lipoate dehydrogenase
-
-
-
-
lipoic acid dehydrogenase
-
-
-
-
NAD(P)H:lipoamide oxidoreductase
NADH:lipoamide oxidoreductase
nicotinamide adenine dinucleotide diaphorase
-
-
CIP50
-
-
coronin-interacting protein
-
-
coronin-interacting protein
-
-
DHLipDH
-
diaphorase
-
-
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
658466, 659099, 659101, 672869, 674382, 675350, 677161, 691569, 694356, 694854, 741757, 764703, 765097, 765743
dihydrolipoamide dehydrogenase
-
674943, 693271, 713452, 741807, 741998, 742087, 742221, 743050, 743051, 743052, 743127, 743767, 765207, 765208, 765209, 765210
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
Starkeyomyces koorchalomoides
-
-
dihydrolipoamide dehydrogenase
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
-
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
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide:NAD+ oxidoreductase
-
-
dihydrolipoamide:NAD+ oxidoreductase
-
DLD
-
DLD1
-
isoform
Dld2
-
isoform
DLDH
-
-
-
-
DLDH2
-
E3
-
-
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E3
-
-
658466, 659099, 659101, 672869, 674382, 674759, 675350, 677161, 691569, 741757, 764703
E3
-
pyruvate dehydrogenase complex is composed of multiple copies of three catalytic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3)
E3
-
674943, 741807, 742221, 743050, 743051, 743052, 743767, 765207, 765208, 765209, 765210
LAD
-
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LADH
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LADH
Starkeyomyces koorchalomoides
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LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity
LADH
Starkeyomyces koorchalomoides FDUS 0337
-
LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity
-
LDH
-
LipDH
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lipoamide dehydrogenase
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-
lipoamide dehydrogenase
-
lipoamide dehydrogenase
-
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lipoamide dehydrogenase
-
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lipoamide dehydrogenase
-
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lipoamide dehydrogenase
-
-
-
lipoamide dehydrogenase
-
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lipoamide dehydrogenase
-
lipoamide dehydrogenase
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
-
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lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
-
lipoamide dehydrogenase C
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lipoamide dehydrogenase C
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lipoamide-dehydrogenase-valine
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-
lipoamide-dehydrogenase-valine
-
is the specific E3 subunit for branched-chain keto acid dehydrogenase
lipoamide-dehydrogenase-valine
-
is the specific E3 subunit for branched-chain keto acid dehydrogenase
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lipoyl dehydrogenase
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-
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-
LPD
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LPD1
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plastidial LPD1 encodes one of the two E3 isoforms found in the plastidial pyruvate dehydrogenase complex
LPD2
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Lpd3
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LpdA
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-
LpdC
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-
LpdG
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LpdV
-
NAD(P)H:lipoamide oxidoreductase
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NAD(P)H:lipoamide oxidoreductase
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NADH dehydrogenase
-
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NADH diaphorase
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NADH:lipoamide oxidoreductase
-
-
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NADH:lipoamide oxidoreductase
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pdhL
-
rhDLDH
-
-
TAase
Starkeyomyces koorchalomoides
-
Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity
TAase
Starkeyomyces koorchalomoides FDUS 0337
-
Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity
-
additional information
-
enzyme is a member of the pyridine nucleotide-disulfide oxidoreductase family of enzymes, enzyme is the E3 component of three different 2-ketoacid dehydrogenase multienzyme complexes, i.e. the pyruvate, 2-ketoglutarate, and branched chain 2-keto acid dehydrogenase complexes
additional information
-
enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
additional information
-
cf. EC 1.6.99.3
additional information
-
cf. EC 1.6.99.3
-
additional information
-
the enzyme is the E3 component of the pyruvate dehydrogenase multienzyme complex
additional information
-
enzyme belongs to the family of pyridine nucleotide oxidoreductases
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(R,S)-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
r
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
1-methoxyphenazinium methosulfate + NADH
? + NAD+
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
cytochrome c is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
2,6-dimethoxy-1,4-benzoquinone + NADH
? + NAD+
8.0% activity compared to lipoamide
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
2-hydroxy-1,4-benzoquinone + NADH
2-hydroxy-1,4-benzoquinol + NAD+
-
-
-
-
?
2-methyl-1,4-benzoquinone + NADH
2-methyl-1,4-benzoquinol + NAD+
-
-
-
-
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
3-nitrotyrosine + NAD(P)H
3-aminotyrosine + NAD(P)+ + H2O
-
-
-
-
?
3-nitrotyrosine + NADPH
3-aminotyrosine + NADP+ + H2O
-
-
-
-
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
5-hydroxy-1,4-naphthoquinone + NADH
5-hydroxy-1,4-naphthoquinol + NAD+
-
-
-
-
?
5-nitroblue tetrazolium chloride + NADH
? + NAD+
-
5.1% of the activity with lipoamide
-
-
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
8-nitroguanine + NAD(P)H
8-aminoguanine + NAD(P)+ + H2O
-
-
-
-
?
8-nitroguanine + NADPH
8-aminoguanine + NADP+ + H2O
-
-
-
-
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
8-nitroxanthine + NAD(P)H
8-aminoxanthine + NAD(P)+ + H2O
-
-
-
-
?
8-nitroxanthine + NADPH
8-aminoxanthine + NADP+ + H2O
-
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
benzyl viologen + NADH
? + NAD+
-
2.9% of the activity with lipoamide
-
-
?
coenzyme Q-10 + NADPH
ubiquinol + NADP+
dihydrolipoamide + NAD+
lipoamide + NADH
dihydrolipoamide + NAD+
lipoamide + NADH + H+
dihydrolipoamide + NADP+
lipoamide + NADPH
-
-
-
r
dihydrolipoate + NAD+
lipoate + NADH + H+
-
-
-
-
r
dihydrolipoic acid + NAD+
lipoic acid + NADH + H+
-
-
-
?
DL-6,8-thiooctic acid amide + NADH
? + NAD+
-
-
-
-
r
DL-alpha-lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
DL-lipoamide + NADH + H+
DL-dihydrolipoamide + NAD+
DL-lipoate + NADH
? + NAD+
-
-
-
-
?
DL-lipoylbutanoate + NADH
? + NAD+
-
-
-
-
?
DL-lipoylpentanoate + NADH
? + NAD+
-
100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state
-
-
?
ferrileghemoglobin + NADH + H+
ferroleghemoglobin + NAD+
-
-
-
r
ferrocene + NADH
? + NAD+
3.6% activity compared to lipoamide
-
-
?
ferrocenecarboxylic acid + NADH
? + NAD+
4.1% activity compared to lipoamide
-
-
?
glycerol trinitrate + NADH
?
hexacyanoferrate + NADH
? + NAD+
-
-
-
-
?
hydroxylamine hydrochloride + NADH
?
iodonitrotetrazolium + NADH
? + NAD+
-
-
-
-
?
iodonitrotetrazolium chloride + NADH
? + NAD+
19.3% activity compared to lipoamide
-
-
?
lipoamide + 3-acetylpyridine adenine dinucleotide
dihydrolipoamide + ?
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
lipoamide + NADH + H+
dihydrolipoamide + NAD+
lipoamide + nicotinamide hypoxanthine dinucleotide
dihydrolipoamide + ?
-
-
-
-
?
lipoamide + thio-NADH
dihydrolipoamide + thio-NAD+
-
-
-
-
?
lipoate + NADH + H+
dihydrolipoate + NAD+
-
-
-
-
r
lipoic acid + NADH
dihydrolipoic acid + NAD+
lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
lipoyl H-protein + NADH + H+
dihydrolipoyl H-protein + NAD+
-
-
-
-
r
mature frataxin + NADH
denoted frataxin + NAD+
menadione + NADH
? + NAD+
methylene blue + NADH
? + NAD+
methylene blue + NADH + H+
reduced methylene blue + NAD+
metmyoglobin + NADH
reduced myoglobin + NAD+
-
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
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
nitrated DNA + NAD(P)H
?
-
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
-
-
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
-
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
-
-
?
nitric oxide + NADH
nitrate + NAD+
-
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
nitrotetrazolium blue + NADH
? + NAD+
2.9% activity compared to lipoamide
-
-
?
nitrotetrazolium blue + NADH + H+
reduced nitrotetrazolium blue + NAD+
-
-
-
-
r
O2 + NADH + H+
H2O2 + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
oxidized lipoamide + NADH
reduced lipoamide + NAD+
-
-
-
-
?
oxidized lipoic acid + NADH
reduced lipoic acid + NAD+
-
-
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
protein N6-(dihydrolipoyl)lysine + NAD+
protein N6-(lipoyl)lysine + NADH + H+
-
-
-
-
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
pyocyanin + NADH + H+
reduced pyocyanin + NAD+
pyocyanin is reported to stimulate respiration
-
-
?
pyruvate + NADH
?
-
-
-
-
?
reduced DL-lipoamide + NAD+
oxidized DL-lipoamide + NADH
-
-
-
-
r
reduced lipoamide + NAD+
oxidized lipoamide + NADH
resazurin + NADH
? + NAD+
155.8% activity compared to lipoamide
-
-
?
resorufin + NADH
? + NAD+
19.1% activity compared to lipoamide
-
-
?
S-nitroso-N-acetylpenicillamine + NADH
?
S-nitrosoglutathione + NADH
?
sodium nitroprusside + NADH
?
sulfonated tetrazolium WST-1 + NADH
formazan derivative + NAD+
39.2% activity compared to lipoamide
-
-
?
tellurite + NADH
NAD+ + ?
thio-NAD+ + NADH
thio-NADH + NAD+
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
vitamin K5 + NADH
?
-
-
-
-
?
additional information
?
-
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
-
-
-
-
?
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
-
-
-
-
?
1-methoxyphenazinium methosulfate + NADH
? + NAD+
248.1% activity compared to lipoamide
-
-
?
1-methoxyphenazinium methosulfate + NADH
? + NAD+
248.1% activity compared to lipoamide
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
31.1% of the activity with lipoamide
-
-
?
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
r
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
-
-
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
-
90fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
-
-
?
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
-
-
-
?
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
-
-
-
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
-
-
-
-
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
-
-
-
-
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
-
-
-
-
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
-
-
-
-
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
-
-
-
-
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
-
-
-
-
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
-
-
-
-
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
-
-
-
-
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
-
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
-
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
-
-
-
-
?
acetaldoxime + NADH
?
-
-
-
-
?
acetaldoxime + NADH
?
-
-
-
-
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
Starkeyomyces koorchalomoides
-
-
-
-
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
?
coenzyme Q-10 + NADPH
ubiquinol + NADP+
-
-
-
-
?
coenzyme Q-10 + NADPH
ubiquinol + NADP+
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
DLDH activity, forward reaction
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
Azotobacter agilis
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
mutant enzymes C44S and C49S show minute activity
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
the forward reaction is the physiological one
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
alternate oxidation and reduction of an intrachain disulfide bond
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
specific substrate
-
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
specific substrate
-
-
?
DL-lipoamide + NADH + H+
DL-dihydrolipoamide + NAD+
-
-
-
-
?
DL-lipoamide + NADH + H+
DL-dihydrolipoamide + NAD+
-
-
-
-
?
formaldoxime + NADH
?
-
-
-
-
?
formaldoxime + NADH
?
-
-
-
-
?
glycerol trinitrate + NADH
?
-
-
-
-
?
glycerol trinitrate + NADH
?
-
-
-
-
?
hydroxylamine hydrochloride + NADH
?
-
-
-
-
?
hydroxylamine hydrochloride + NADH
?
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
NADH:lipoamide oxidoreductase activity, reverse reaction
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
100% activity
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
100% activity
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
?
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
r
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
r
lipoic acid + NADH
dihydrolipoic acid + NAD+
-
-
-
-
?
lipoic acid + NADH
dihydrolipoic acid + NAD+
-
-
-
r
lipoic acid + NADH
dihydrolipoic acid + NAD+
-
-
-
-
?
lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
-
r
lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
-
r
mature frataxin + NADH
denoted frataxin + NAD+
-
cleavage by C-term DLD
-
-
?
mature frataxin + NADH
denoted frataxin + NAD+
-
cleavage by C-term DLD
-
-
?
mature frataxin + NADH
denoted frataxin + NAD+
-
exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity
-
-
?
menadione + NADH
? + NAD+
2.9% activity compared to lipoamide
-
-
?
menadione + NADH
? + NAD+
2.9% activity compared to lipoamide
-
-
?
menadione + NADH
? + NAD+
-
13.6% of the activity with lipoamide
-
-
?
methylene blue + NADH
? + NAD+
-
-
-
-
?
methylene blue + NADH
? + NAD+
-
9.4% of the activity with lipoamide
-
-
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
-
-
-
-
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
-
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
-
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
-
-
-
-
?
O2 + NADH
?
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
O2 + NADH
H2O2 + NAD+
-
-
-
-
?
O2 + NADH
H2O2 + NAD+
-
40fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
-
-
?
O2 + NADH
H2O2 + NAD+
-
-
-
-
?
O2 + NADH
H2O2 + NAD+
-
the enzyme produces reactive oxygen species, i.e. hydrogen peroxide, acting as an oxidase
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
233.4% activity compared to lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
233.4% activity compared to lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
12.3% of the activity with lipoamide
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
-
-
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
-
-
-
r
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes
-
-
r
S-nitroso-N-acetylpenicillamine + NADH
?
-
-
-
-
?
S-nitroso-N-acetylpenicillamine + NADH
?
-
-
-
-
?
S-nitrosoglutathione + NADH
?
-
-
-
-
?
S-nitrosoglutathione + NADH
?
-
-
-
-
?
sodium nitroprusside + NADH
?
-
-
-
-
?
sodium nitroprusside + NADH
?
-
-
-
-
?
tellurite + NADH
NAD+ + ?
-
-
-
-
?
tellurite + NADH
NAD+ + ?
-
-
-
-
?
tellurite + NADH
NAD+ + ?
-
-
-
?
tellurite + NADH
NAD+ + ?
-
-
-
?
tellurite + NADH
NAD+ + ?
-
-
-
?
thio-NAD+ + NADH
thio-NADH + NAD+
-
-
-
-
?
thio-NAD+ + NADH
thio-NADH + NAD+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
thio-NAD+ + NADH
thio-NADH + NAD+
-
-
-
-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
-
-
-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
-
-
-
ir
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
-
-
?
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
-
-
-
?
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
additional information
?
-
-
NADH:NAD+ transhydrogenase activity
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
?
additional information
?
-
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
?
additional information
?
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the most important function of dehydrolipoamide dehydrogenase as a component of the pyruvate dehydrogenase and the 2-oxoglutarate dehydrogenase complex is the implication in the oxidative decarboxylation of pyruvate and 2-oxoglutarate
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is one of the major antigens for production of autoantibodies after infection with hepatitis C virus causing autoimmune phenomena like higher prevalences for liver cirrhosis, arthritis, abnormal liver function, and elevated alpha-FP levels, immunocolorimetrical determination of anti-E3 antibody titer after infection in several patients and of clinical manifestations, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the reoxidation of the covalently bound reduced lipoic acid cofactor of the E2 subunits of all the mitochondrial alpha-keto acid dehydrogenase multienzyme complexes including the alpha-ketoglutarate dehydrogenase complex, the pyruvate dehydrogenase complex, and the branched-chain alpha-keto acid dehydrogenase complex
-
-
-
additional information
?
-
-
the enzyme also shows diaphorase activity with 2,6-dichlorophenol indophenol and thiazolyl blue tetrazolium bromide
-
-
-
additional information
?
-
-
the enzyme also shows diaphorase activity with 2,6-dichlorophenol indophenol and thiazolyl blue tetrazolium bromide
-
-
-
additional information
?
-
-
DLD catalyzes the reduction of NAD+ by dihydrolipoamide and exhibits NADH-dependent diaphorase activity
-
-
?
additional information
?
-
-
DLD catalyzes the reduction of NAD+ by dihydrolipoamide and exhibits NADH-dependent diaphorase activity
-
-
?
additional information
?
-
-
diaphorase activity
-
-
?
additional information
?
-
enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosphorylation, overview
-
-
?
additional information
?
-
-
the enzyme is required for hyperactivation, i.e. enhanced motility, and acrosome reaction of hamster spermatozoa, the post-pyruvate metabolic enzyme shows dual involvement and regulation during sperm capacitation, control of the directionality of enzyme activity during sperm capacitation
-
-
?
additional information
?
-
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
?
additional information
?
-
-
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
?
additional information
?
-
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
?
additional information
?
-
-
reductive half-reaction, hydride transfer from NADH to FAD, is rate limiting when a quinone is the oxidant
-
-
?
additional information
?
-
-
EC 1.8.1.4 is the E3-protein component of the mitochondrial 2-oxoacid dehydrogenase multienzyme complexes and the L-protein component of the glycine decarboxylase system
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the physiological substrates are the dihydrolipoyl domain of the E2 component, dihydrolipoyl acyltransferase, of the 2-oxoacid dehydrogenase multienzyme complexs or the dihydrolipoyl H-protein of the mitochobdrial glycine decarboxylase
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
enzyme lacks diaphorase activity
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
diaphorase activity
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme might play a role in modifying NO levels under specific cell conditions
-
-
?
additional information
?
-
-
LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
-
-
?
additional information
?
-
-
the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
dihydrolipoamide + NAD+
lipoamide + NADH
dihydrolipoamide + NAD+
lipoamide + NADH + H+
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
r
nitrated DNA + NAD(P)H
?
-
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
-
-
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
-
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
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
protein N6-(dihydrolipoyl)lysine + NAD+
protein N6-(lipoyl)lysine + NADH + H+
-
-
-
-
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes
-
-
r
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
additional information
?
-
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
the forward reaction is the physiological one
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
r
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
-
-
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
-
-
-
ir
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
?
additional information
?
-
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
?
additional information
?
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the most important function of dehydrolipoamide dehydrogenase as a component of the pyruvate dehydrogenase and the 2-oxoglutarate dehydrogenase complex is the implication in the oxidative decarboxylation of pyruvate and 2-oxoglutarate
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is one of the major antigens for production of autoantibodies after infection with hepatitis C virus causing autoimmune phenomena like higher prevalences for liver cirrhosis, arthritis, abnormal liver function, and elevated alpha-FP levels, immunocolorimetrical determination of anti-E3 antibody titer after infection in several patients and of clinical manifestations, overview
-
-
?
additional information
?
-
enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosphorylation, overview
-
-
?
additional information
?
-
-
the enzyme is required for hyperactivation, i.e. enhanced motility, and acrosome reaction of hamster spermatozoa, the post-pyruvate metabolic enzyme shows dual involvement and regulation during sperm capacitation, control of the directionality of enzyme activity during sperm capacitation
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the physiological substrates are the dihydrolipoyl domain of the E2 component, dihydrolipoyl acyltransferase, of the 2-oxoacid dehydrogenase multienzyme complexs or the dihydrolipoyl H-protein of the mitochobdrial glycine decarboxylase
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme might play a role in modifying NO levels under specific cell conditions
-
-
?
additional information
?
-
-
the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,3-bis(2-chloroethyl)-1-nitrourea
-
after reduction of the oxidized form of enzyme to the two-electron-reduced state
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
at higher concentrations (2 mM) significantly inhibits the lipoamide dehydrogenase activity
1-methyl-4-phenylpyridinium
-
at lower concentrations (1 mM) as compared to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine significantly inhibits the lipoamide dehydrogenase activity
10-(2-dimethylaminopropyl)-dibenzothiazine cation radical
-
60% inactivation after 10 min incubation and 79% after 30 min using the myeloperoxidase system, 72% inactivation after 10 min incubation using the horseradish peroxidase system
10-(2-methyl,3-dimethylaminopropyl)-dibenzothiazine cation radical
-
90% inactivation after 10 min and 30 min incubation using the myeloperoxidase system, 94% inactivation after 10 min incubation using the horseradish peroxidase system
10-(3-dimethylaminopropyl)-dibenzothiazine cation radical
-
87% inactivation after 10 min incubation and 89% after 30 min using the myeloperoxidase system, 94% inactivation after 10 min incubation using the horseradish peroxidase system
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine hydrochloride
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-amino-4-hydroxy-6-methyl-7,8-dihydropteridine
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-chloro-10-(3-dimethylaminopropyl)-dibenzothiazine cation radical
-
45% inactivation after 10 min incubation and 75% after 30 min using the myeloperoxidase system, 89% inactivation after 10 min incubation using the horseradish peroxidase system
2-chloro-10-[3-(1-methyl-4-piperazinyl)-propyl]-dibenzothiazine cation radical
-
54% inactivation after 10 min incubation and 80% after 30 min using the myeloperoxidase system, 90% inactivation after 10 min incubation using the horseradish peroxidase system
2-chloro-10-[3-[1-(2-hydroxyethyl)-4-piperazinyl]propyl]-dibenzothiazine cation radical
-
42% inactivation after 10 min incubation and 69% after 30 min using the myeloperoxidase system, 79% inactivation after 10 min incubation using the horseradish peroxidase system
2-methylmercapto-10-[2-(1-methyl-2-piperidinyl)-ethyl]-dibenzothiazine cation radical
-
77% inactivation after 10 min incubation and 82% after 30 min using the myeloperoxidase system, 85% inactivation after 10 min incubation using the horseradish peroxidase system
2-propionyl-10-(3-dimethylaminopropyl)-dibenzothiazine cation radical
-
11% inactivation after 10 min incubation and 32% after 30 min using the myeloperoxidase system, 83% inactivation after 10 min incubation using the horseradish peroxidase system
2-trifluoromethyl-10-[3-(1-methyl-4-piperazinyl)propyl]-dibenzothiazine cation radical
-
5% inactivation after 10 min incubation and 16% after 30 min using the myeloperoxidase system, 67% inactivation after 10 min incubation using the horseradish peroxidase system
2-trifluoromethyl-10-[3-(dimethylamino)propyl]-dibenzothiazine cation radical
-
2% inactivation after 10 and 30 min incubation using the myeloperoxidase system, 16% inactivation after 10 min incubation using the horseradish peroxidase system
2-trifluoromethyl-10-[3-[1-(2-hydroxyethyl)4-piperazinyl]propyl]-dibenzothiazine cation radical
-
1% inactivation after 10 min incubation and 8% after 30 min using the myeloperoxidase system, 61% inactivation after 10 min incubation using the horseradish peroxidase system
2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]-N-[3-(trifluoromethyl)benzyl]acetamide
-
5-methoxyindole-2-carboxylic acid
Angeli's salt
-
at 2 mM, induces a 90% loss in DLDH diaphorase activity
Cd2+
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
chlorpromazine
-
0.1 mM, 75% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 94% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 89% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
cyanide
slight inhibition; slight inhibition; slight inhibition
Diethylamine NONOate
-
induces 71% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
diisopropyl fluorophosphate
diphenyleneiodonium
an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro; an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro; an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro
diphenyleneiodonium chloride
Fe2+
-
at high concentrations has significant inhibitory effect on the lipoamide dehydrogenase activity
fluphenazine
-
0.1 mM, 53% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 61% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
folic acid
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
Guanidine-HCl
-
4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible
H2O2
-
enzyme is inactivated by complex III- but not complex I-derived reactive oxygen species, and the accompanying loss of activity due to the inactivation can be restored by cysteine and glutathione. H2O2 instead of superoxide anion is responsible for the inactivation, and protein sulfenic acid formation is associated with the loss of enzymatic activity
Hg2+
1 mM shows strong inhibitory effect on recombinant rBfmBC activity (more than 80% inhibition)
iodoacetic acid
-
in presence of NADH or dihydrolipoamide
isobiopterin
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
N-[2-(2,4-dichlorophenyl)ethyl]-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]acetamide
most potent inhibitor, noncompetitive versus NADH, NAD+, and lipoamide
NAD(P)+
-
product inhibition
p-Aminophenyldichloroarsine
p-[(bromoacetyl)-amino]phenyl arsenoxide
-
irreversible active site directed inactivation
Pb2+
1 mM shows strong inhibitory effect on recombinant BfmBC activity (more than 80% inhibition)
PCMB
-
0.1 mM, 50% inhibition
perphenazine
-
0.1 mM, 69% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 75% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 79% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
phenothiazine cation radicals
-
irreversible inactivation dependent on time, radical structure, and radical production enzyme system, radicals are produced by reaction of myeloperoxidase or horse radish peroxidase on the phenothiazines promazine, trimeprazine, thioridazine, chlorpromazine, prochlorperazine, promethazine, and others, in presence of H2O2, protection by radical scavengers e.g. thiol compounds, amino acids and peptides, pyridine dinucleotides like NADH, or best by ascorbate and trolox, overview
potassium phosphate
-
when purified DLDH is eluted directly into potassium phosphate buffer, the enzymatic activity rapidly decreases
prochlorperazine
-
0.1 mM, 80% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 85% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 80% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
promazine
-
0.1 mM, 89% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 93% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 94% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4, 94% inhibition in the presence of 0.2 mM NADH, 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 after 10 min incubation
Promethazine
-
0.1 mM, 79% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 51% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 72% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
propericyazine
-
0.1 mM, 40% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4
propionylpromazine
-
0.1 mM, 32% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 88% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 83% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
S-nitrosocysteine
-
induces a 62% loss in diaphorase activity at 2 mM and an 88% loss at 10 mM
S-nitrosoglutathione
-
induces 84% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
thioridazine
-
0.1 mM, 82% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 97% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 85% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4, 85% inhibition in the presence of 0.1 mM NADH, 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 after 10 min incubation
Trifluoperazine
-
0.1 mM, 16% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 72% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 67% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
triflupromazine
-
0.1 mM, 68% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 16% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
trimeprazine
-
0.1 mM, 90% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 90% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 94% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
valproyl-CoA
-
competitive inhibitor, 0.5-1.0 mM inhibit DLDH activity
valproyl-dephosphoCoA
-
uncompetitive inhibitor, 0.5-1.0 mM inhibit DLDH activity
5-methoxyindole-2-carboxylic acid
-
5-methoxyindole-2-carboxylic acid
specific inhibitor, inhibition in vivo blocks acrosome reaction completely and hyperactivation partially
5-methoxyindole-2-carboxylic acid
-
specific inhibitor of DLD, dibutryl cyclic adenosine monophosphate and the calcium ionophore A23187 can significantly reverse the inhibitory effect on sperm acrosome reaction
arsenite
activity of lipoamide dehydrogenase in isolated mitochondria is sensitive to arsenite, but not arsenate
arsenite
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
arsenite
-
reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity
arsenite
-
0.3 mM, 50% inhibition
diisopropyl fluorophosphate
-
fully inhibits activity of the C-term protein
diisopropyl fluorophosphate
-
DLD is fully inactivated by 1 mM
diisopropyl fluorophosphate
-
DLD is fully inactivated by 1 mM
diphenyleneiodonium chloride
-
-
diphenyleneiodonium chloride
-
-
N-ethylmaleimide
-
induces more than 95% loss in DLDH diaphorase activity
N-ethylmaleimide
-
over 90% inhibition at 1 mM
NAD+
-
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
NAD+
-
product inhibition of the oxygen oxidase activity
NADH
strong substrate inhibition at concentrations higher than 0.015 mM
NADH
-
competitive with respect to NAD+
NADH
-
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
NADH
-
chloroplastic enzyme is more susceptible to product inhibition than the mitochondrial enzyme
NADH
-
competitive with respect to NAD+
p-Aminophenyldichloroarsine
-
-
p-Aminophenyldichloroarsine
-
inactivated only in presence of NADH and dihydrolipoamide, no significant loss of activity in absence of NADH and dihydrolipoamide
p-Aminophenyldichloroarsine
-
in presence of NADH
Zn2+
about 30% inhibition of recombinant BfmBC activity with 5 mM
Zn2+
-
reversible binding, competitive to lipoamide, uncompetitive to NADH
additional information
-
LAD is not inhibited by resorufin ethyl ether, phenidone, Nomega-nitro-L-arginine methyl ester hydrochloride, proadiphen hydrochloride, and miconazole nitrate
-
additional information
Nutlin-3 inhibits mitochondrial activity
-
additional information
-
calcium and copper do not affect the enzyme activity
-
additional information
-
expression of LRG-47, as well as IFNgamma stimulation, block intracellular interaction of coronin-1 with LpdC
-
additional information
-
expression of LRG-47, as well as IFNgamma stimulation, block intracellular interaction of coronin-1 with LpdC
-
additional information
-
diamide, GSH, GSSG, cysteine and nitrite do not exhibit any inhibitory effects
-
additional information
-
no age-related decline in DLDH activity or expression is evident in rats over the period from 5 to 30 months of age. Lower DLDH dehydrogenase activity observed in pups may be due to NADH inhibition
-
additional information
-
enzyme is sensitive to air-inactivation
-
additional information
-
inhibited by caloric restriction
-
additional information
-
no inhibition by iodoacetate
-
additional information
-
no inhibition of the nitric oxide reduction by cyanide, antimycin A, or diphenyleneiodonium ions
-
additional information
-
LAD is not inhibited by resorufin ethyl ether, phenidone, Nomega-nitro-L-arginine methyl ester hydrochloride, proadiphen hydrochloride, and miconazole nitrate
-
additional information
-
no inhibition by the cation radical of 2-cyano-10-[3-(4-hydroxypiperidinyl)propyl]-dibenzothiazine in either peroxidase system
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.01 - 0.4
1,4-benzoquinone
0.05
1,4-Naphthoquinone
-
-
0.015 - 0.12
2,6-dichlorophenolindophenol
0.86
2,6-dimethyl-1,4-benzoquinone
-
-
0.46 - 1.45
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
0.39
3-acetylpyridine adenine dinucleotide
-
-
0.29
5-hydroxy-1,4-naphthoquinone
-
-
0.96
acetaldoxime
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
3.63
alpha-lipoamide
Starkeyomyces koorchalomoides
-
in 0.1 mM Tris-HCl (pH 7.0), 0.0005 mM EDTA, 0.01 mM beta2-mercaptoethanol, at 37°C
0.0107 - 43.6
dihydrolipoamide
0.029
ferrileghemoglobin
-
2.73 - 17.82
formaldoxime
0.9 - 16.93
glycerol trinitrate
3.24
Hydroxylamine hydrochloride
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.027
lipoyl H-protein
-
-
-
0.35
NADPH
-
recombinant DiaA
2.6
nicotinamide hypoxanthine dinucleotide
-
-
0.5
nitrotetrazolium blue
-
recombinant DiaA
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
0.036
thio-NAD+
-
reaction with NADH
additional information
additional information
-
0.01
1,4-benzoquinone
-
-
0.015
2,6-dichlorophenolindophenol
-
-
0.03
2,6-dichlorophenolindophenol
-
-
0.12
2,6-dichlorophenolindophenol
in diaphorase activity
0.46
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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
0.0107
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423A
0.0157
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI
0.017
dihydrolipoamide
-
-
0.0177
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI
0.018
dihydrolipoamide
pH 8.0, 37°C
0.0228
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423Q
0.023
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423S
0.0243
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.025
dihydrolipoamide
-
-
0.0266
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423D
0.0269
dihydrolipoamide
pH 7.0, 30°C, wild-type enzyme
0.027
dihydrolipoamide
enzyme mutant, pH 8.0, 37°C
0.0274
dihydrolipoamide
pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI
0.031
dihydrolipoamide
mutant enzyme P387A, at pH 8.0 and 37°C
0.0364
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI
0.04
dihydrolipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain
0.046
dihydrolipoamide
37°C, pH 8.0
0.05
dihydrolipoamide
-
mutant enzyme S53K/K54S
0.056
dihydrolipoamide
-
recombinant DLDH
0.064
dihydrolipoamide
-
recombinant DLDH expressed without lipoic acid
0.08
dihydrolipoamide
-
complex-bound dihydrolipoamide dehydrogenase
0.09
dihydrolipoamide
-
mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.12
dihydrolipoamide
-
mutant enzyme E192Q
0.12
dihydrolipoamide
mutant R281K
0.13
dihydrolipoamide
-
-
0.146
dihydrolipoamide
-
pH 8.0, 25°C, mitochondrial isozyme
0.16
dihydrolipoamide
enzyme mutant C50T, pH 8.0, 37°C
0.16
dihydrolipoamide
enzyme mutant H329A, pH 8.0, 37°C
0.19
dihydrolipoamide
wild-type enzyme, pH 8.0, 37°C
0.2
dihydrolipoamide
mutant enzyme N286Q
0.2
dihydrolipoamide
mutant N286Q
0.22
dihydrolipoamide
enzyme mutant C50A, pH 8.0, 37°C
0.28
dihydrolipoamide
-
free dihydrolipoamide dehydrogenase
0.31
dihydrolipoamide
mutant enzyme L99A, at pH 8.0 and 37°C
0.38
dihydrolipoamide
wild-type
0.38
dihydrolipoamide
wild type enzyme
0.38
dihydrolipoamide
mutant R281N
0.38
dihydrolipoamide
wild-type E3
0.48
dihydrolipoamide
-
-
0.52
dihydrolipoamide
mutant enzyme P355A, at pH 8.0 and 37°C
0.55
dihydrolipoamide
enzyme mutant P303A, pH 8.0, 37°C
0.58
dihydrolipoamide
mutant T148G
0.58
dihydrolipoamide
-
mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.59
dihydrolipoamide
mutant T148S
0.63
dihydrolipoamide
wild-type enzyme, pH 8.0, 37°C
0.63
dihydrolipoamide
enzyme mutant P156A, pH 8.0, 37°C
0.64
dihydrolipoamide
wild-type enzyme, pH 8.0, 37°C
0.64
dihydrolipoamide
wild type enzyme, at pH 8.0 and 37°C
0.64
dihydrolipoamide
-
wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.69
dihydrolipoamide
-
native enzyme
0.7
dihydrolipoamide
mutant enzyme N286D
0.7
dihydrolipoamide
mutant N286D
0.7
dihydrolipoamide
mutant enzyme P423A, at pH 8.0 and 37°C
0.76
dihydrolipoamide
-
mutant enzyme K37E
0.8299
dihydrolipoamide
-
enzyme variant 2, at pH 7.5 and 37°C
0.83
dihydrolipoamide
-
-
0.87
dihydrolipoamide
mutant enzyme P154A, at pH 8.0 and 37°C
0.88
dihydrolipoamide
-
wild-type enzyme
1.15
dihydrolipoamide
-
mutant enzyme A48I, at pH 7.5 and 37°C
1.16
dihydrolipoamide
-
pH 8.0, 25°C, recombinant His-tagged enzyme
1.21
dihydrolipoamide
mutant enzyme D320N
1.21
dihydrolipoamide
mutant D320N
2.2
dihydrolipoamide
-
mutant enzyme D49G, at pH 7.5 and 37°C
2.7
dihydrolipoamide
-
enzyme variant 1, at pH 7.5 and 37°C
2.9
dihydrolipoamide
-
mutant enzyme H457Q
3.56
dihydrolipoamide
-
wild type enzyme, at pH 7.5 and 37°C
3.9
dihydrolipoamide
-
mutant enzyme C38G, at pH 7.5 and 37°C
4.7
dihydrolipoamide
-
mutant enzyme A54I, at pH 7.5 and 37°C
18.4
dihydrolipoamide
-
mutant enzyme C15T, at pH 7.5 and 37°C
43.6
dihydrolipoamide
-
mutant enzyme H452Q
2.73
formaldoxime
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
15.83
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
17.18
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
17.82
formaldoxime
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.9
glycerol trinitrate
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.42
glycerol trinitrate
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.27
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
16.93
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.05
Lipoamide
mutant enzyme N286Q
0.05
Lipoamide
mutant N286Q
0.07
Lipoamide
mutant enzyme N286D
0.07
Lipoamide
mutant N286D
0.31
Lipoamide
-
mutant enzyme E192Q
0.46
Lipoamide
mutant enzyme D320N
0.46
Lipoamide
mutant D320N
0.56
Lipoamide
wild type enzyme
0.56
Lipoamide
-
reaction with 3-acetylpyridine adenine dinucleotide
0.63
Lipoamide
-
mutant enzyme S53K/K54S
0.841
Lipoamide
-
pH 7.0, 25°C, recombinant His-tagged enzyme
0.87
Lipoamide
-
pH 8.0, 25°C, mitochondrial isozyme
2.25
Lipoamide
-
wild-type enzyme
3.3
Lipoamide
in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
5
Lipoamide
-
mutant enzyme K54E
5.8
Lipoamide
-
reaction with thio-NADH
6.4
Lipoamide
-
reaction with nicotinamide hypoxanthine dinucleotide
16
Lipoamide
-
reaction with NADH
2.9
lipoate
-
-
2.1
lipoic acid
-
-
0.024
NAD+
enzyme mutant, pH 8.0, 37°C
0.035
NAD+
mutant enzyme P387A, at pH 8.0 and 37°C
0.045
NAD+
-
pH 8.0, 25°C, mitochondrial isozyme
0.06
NAD+
-
mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.096
NAD+
-
pH 8.0, 25°C, recombinant His-tagged enzyme
0.1 - 0.11
NAD+
-
chloroplastic enzyme
0.156
NAD+
pH 7.0, 30°C, wild-type enzyme
0.16
NAD+
mutant enzyme N286Q
0.17123
NAD+
-
enzyme variant 1, at pH 7.5 and 37°C
0.182
NAD+
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.186
NAD+
pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI
0.19
NAD+
wild-type enzyme, pH 8.0, 37°C
0.19
NAD+
wild type enzyme, at pH 8.0 and 37°C
0.19
NAD+
-
mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.19
NAD+
-
wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.199
NAD+
pH 7.0, 30°C, mutant enzyme E423D
0.2
NAD+
enzyme mutant C50T, pH 8.0, 37°C
0.203
NAD+
pH 7.0, 30°C, mutant enzyme E423Q
0.211
NAD+
pH 7.0, 30°C, mutant enzyme E423S
0.215
NAD+
pH 7.0, 30°C, mutant enzyme E423A
0.22
NAD+
wild type enzyme
0.24
NAD+
enzyme mutant P156A, pH 8.0, 37°C
0.25
NAD+
-
mutant enzyme K37E
0.266
NAD+
-
enzyme variant 2, at pH 7.5 and 37°C
0.27
NAD+
mutant enzyme P154A, at pH 8.0 and 37°C
0.288
NAD+
pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI
0.29
NAD+
enzyme mutant H329A, pH 8.0, 37°C
0.292
NAD+
pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI
0.3
NAD+
mutant enzyme N286D
0.31
NAD+
-
mutant enzyme E192Q
0.312
NAD+
pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI
0.32
NAD+
-
native enzyme and mutant enzyme E457Q
0.34
NAD+
mutant enzyme D320N
0.38
NAD+
-
mutant enzyme H452Q
0.4
NAD+
-
wild-type enzyme
0.4
NAD+
-
complex-bound dihydrolipoamide dehydrogenase
0.4
NAD+
mutant enzyme P423A, at pH 8.0 and 37°C
0.42
NAD+
enzyme mutant P303A, pH 8.0, 37°C
0.43
NAD+
-
wild type enzyme, at pH 7.5 and 37°C
0.47
NAD+
enzyme mutant C50A, pH 8.0, 37°C
0.55
NAD+
-
mutant enzyme S53K/K54S
0.62 - 0.64
NAD+
-
mitochondrial enzyme
0.64
NAD+
wild-type enzyme, pH 8.0, 37°C
0.7
NAD+
mutant enzyme P355A, at pH 8.0 and 37°C
0.82
NAD+
-
recombinant DLDH expressed without without a lipoyl protein domain
0.98
NAD+
-
mutant enzyme A48I, at pH 7.5 and 37°C
0.985
NAD+
-
recombinant DLDH expressed without lipoic acid
1.037
NAD+
-
recombinant DLDH
1.3
NAD+
mutant enzyme L99A, at pH 8.0 and 37°C
1.31
NAD+
-
mutant enzyme A54I, at pH 7.5 and 37°C
1.43
NAD+
-
mutant enzyme C15T, at pH 7.5 and 37°C
1.5
NAD+
-
mutant enzyme D49G, at pH 7.5 and 37°C
1.83
NAD+
-
free dihydrolipoamide dehydrogenase
4.1
NAD+
-
mutant enzyme C38G, at pH 7.5 and 37°C
0.00315
NADH
-
0.0041
NADH
-
reaction with thio-NAD+
0.0061
NADH
in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
0.0084
NADH
-
reaction with O2
0.0085
NADH
-
NADH:2,6-dichlorophenol indophenol reductase activity
0.009
NADH
-
NADH:NAD+ transhydrogenase activity
0.01
NADH
-
lipoamide dehydrogenase activity
0.01
NADH
-
nitric oxide reduction, pH 7.5
0.015
NADH
-
pH 7.0, 25°C, recombinant His-tagged enzyme
0.021
NADH
-
pH 8.0, 25°C, mitochondrial isozyme
0.04
NADH
wild type enzyme
0.071
NADH
-
mutant enzyme E192Q
0.13
NADH
-
mutant enzyme S53K/K54S
0.13
NADH
mutant enzyme N286D
0.14
NADH
mutant enzyme N286Q
0.15
NADH
-
recombinant DiaA
0.156
NADH
-
reaction with 2,6-dimethyl-1,4-benzoquinone
0.161
NADH
-
reaction with 5-hydroxy-1,4-naphthoquinone
0.24
NADH
mutant enzyme D320N
0.25
NADH
in diaphorase activity
6.2
NADH
-
reaction with lipoic acid
84
NADH
-
reaction with lipoamide
0.3
pyruvate
-
mutant E354K
0.4
pyruvate
-
native LPD
0.48
pyruvate
-
mutant H322Y
0.42
S-nitroso-N-acetylpenicillamine
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
5.48
S-nitroso-N-acetylpenicillamine
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.12
S-nitrosoglutathione
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.44
S-nitrosoglutathione
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.84
sodium nitroprusside
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.26
sodium nitroprusside
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
additional information
additional information
-
dehydrogenase and oxidase activity kinetics
-
additional information
additional information
-
ping pong kinetics
-
additional information
additional information
-
transient-state and steady-state kinetics of the enzyme in two-electron-reduced and four-electron-reduced state at 4°C and 25°C, respectively
-
additional information
additional information
-
transient-state kinetics of reductive and oxidative half-reactions
-
additional information
additional information
enzyme kinetic analysis
-
additional information
additional information
kinetic analysis and mechanisms of wild-type and mutant enzymes, overview
-
additional information
additional information
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
kinetic analysis and modelling, detailed overview
-
additional information
additional information
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
kinetic analysis and modelling, detailed overview
-
additional information
additional information
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
Michaelis?Menten kinetics
-
additional information
additional information
Michaelis?Menten kinetics
-
additional information
additional information
-
Michaelis?Menten kinetics
-
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evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
E3 belongs to the pyridine nucleotide-disulfide oxidoreductase family along with glutathione reductase (GR), thioredoxin reductase, mercuric reductase and trypanothione reductase
evolution
residue Cys50 is absolutely conserved, Cys50 is a component of the very long a-helix structure 2, which is composed of 25 amino acids. Residue Cys50 forms an active disulfide center with Cys45
evolution
residue H329 is absolutely conserved, H329 329 is a part of the long alpha-helix 8, which is composed of 16 amino acids and is a component of the central domain. His329 is also located near FAD and the active disulfide center between Cys45 and Cys50, which are essential to the catalytic activity of human E3
evolution
residues Pro156 and Pro303 are highly conserved
malfunction
-
enhanced arsenate and arsenite sensitivity is due to the disruption of the plastidial LPD1 and LPD2 genes
malfunction
-
the homozygous deletion mutant lpd1/lpd1 is unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibits a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5 mM of hydrogen peroxide and shows filamentation defects
malfunction
as a common component in three 2-oxo acid dehydrogenase, a decrease in E3 activity affects the activities of all three complexes, which leads to increased urinary excretion of 2-oxo acids, elevated blood lactate, pyruvate, and branched chain amino acids. Patients with an E3 deficiency normally die young because an E3 deficiency is a critical genetic defect affecting the central nervous system. A deficiency in E3 results in Leigh syndrome with recurrent episodes of hypoglycemia and ataxia, permanent lactic acidaemia, and mental retardation. A C45A mutation results in a large decrease in human E3 activity and changes in the spectroscopic properties of human E3
malfunction
metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial lipoamide dehydrogenase2. Both arsenate and arsenite inhibit root elongation, decreased seedling size and increase anthocyanin production more profoundly in knockout mutants than in wild-type seedlings, arsenite seems to be the mediator of the observed phenotypes
malfunction
pathogenic amino acid substitutions of the common E3 component (hE3) of the human 2-oxoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause premature death. Determination of structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase involved in E3 deficiency, using hydrogen/deuterium-exchange mass spectrometry
malfunction
pathogenic mutations of hLADH cause severe metabolic diseases (atypical forms of E3 deficiency) that often escalate to cardiological or neurological presentations and even premature death. The pathologies are generally accompanied by lactic acidosis. hLADH presents a distinct conformation under acidosis (pH 5.5-6.8) with lower physiological activity and the capacity of generating reactive oxygen species (ROS). Molecular dynamics simulation of the structural changes induced in the low-pH conformation of hLADH by five pathogenic mutations of hLADH. Determination of structures of these disease-causing mutants of hLADH, overview
malfunction
-
pathogenic mutations of LADH cause severe metabolic disturbances, called E3 deficiency that often involve cardiological and neurological symptoms and premature death. Some of the known pathogenic mutations augment the reactive oxygen species (ROS) generation capacity of LADH, which may contribute to the clinical presentations. Structural changes are likely to turn the physiological LADH conformation to its ROS-generating conformation
malfunction
-
Pfae3 is deleted from Plasmodium falciparum and although the mutants are viable, they display a highly synchronous growth phenotype during intra-erythrocytic development. The mutants also show changes in the expression of some mitochondrial and antioxidant proteins suggesting that deletion of Pfae3 impacts on the parasite's metabolic function with downstream effects on the parasite's redox homoeostasis and cell cycle
malfunction
chronic inhibition of the enzyme can attenuate oxidative stress in type 2 diabetes
malfunction
-
the homozygous deletion mutant lpd1/lpd1 is unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibits a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5 mM of hydrogen peroxide and shows filamentation defects
-
metabolism
-
enzyme is inactivated by complex III- but not complex I-derived reactive oxygen species, and the accompanying loss of activity due to the inactivation can be restored by cysteine and glutathione. H2O2 instead of superoxide anion is responsible for the inactivation, and protein sulfenic acid formation is associated with the loss of enzymatic activity
metabolism
dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxoglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions
metabolism
dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxoglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions
metabolism
dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxooglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions
metabolism
the enzyme is a key enzyme in oxidative metabolism
physiological function
-
effects of insulin treatment on HuC/HuD myoenteric neurons, NADH diaphorase, and nNOS-positive myoenteric neurons of the duodenum of adult rats with acute diabetes is investigated: The density of NADH diaphorase-positive neurons in animals from the diabetic group and in the insulin treated diabetic group is greater than in the control group, indicating that short-term diabetes increases the activity of respiratory chain enzymes
physiological function
-
last step of glycine cleavage system
physiological function
dihydrolipoamide dehydrogenase is a FAD-linked subunit of 2-oxooglutarate, pyruvate and branched-chain amino acid dehydrogenases and the glycine cleavage system, transfering electrons from the dihydrolipoic acid prosthetic group to the NAD+ cofactor via its FAD center
physiological function
-
dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
physiological function
LPD is a useful biocatalyst for regenerating NAD+
physiological function
-
plastidial LPD expression quantitatively controls Arabidopsis arsenate sensitivity
physiological function
Starkeyomyces koorchalomoides
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
physiological function
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
physiological function
-
like the raffinose ATP-binding protein RafK, the presence of the enzyme also activates the expression of raf operon genes. Enzyme-negative pneumococci show a significantly decreased expression of aga and rafEFG, but dihydrolipoamide dehydrogenase does not regulate rafK or the putative regulatory genes rafR and rafS. Dihydrolipoamide dehydrogenase also binds directly to RafK both in vitro and in vivo, indicating the possibility that dihydrolipoamide dehydrogenase regulates raffinose transport by a direct interaction with the regulatory domain of the transporter
physiological function
-
lipoamide dehydrogenase-deficient Mycobacterium tuberculosis is severely attenuated in wild type and immunodeficient mice. When dihydrolipoamide acyltransferase is absent, Mycobacterium tuberculosis upregulates an lipoamide dehydrogenase-dependent branched chain keto-acid dehydrogenase encoded by pdhA, pdhB, pdhC and lpdC. Without lipoamide dehydrogenase, Mycobacterium tuberculosis cannot metabolize branched chain amino acids and potentially toxic branched chain intermediates accumulate. Mycobacterium tuberculosis deficient in both dihydrolipoamide acyltransferase and pdhC phenocopies lipoamide Mycobycterium tuberculosis
physiological function
-
RNA interference or the deletion of both alleles of lipoamide dehydrogenase in bloodstream Trypanosoma brucei results in an absolute requirement for exogenous thymidine. In the absence of thymidine, lipdh-/- parasites show a severely altered morphology and cell cycle distribution. Lipdh-/- cells are unable to infect mice. Degradation of branched-chain amino acids takes place but is dispensable. In cultured bloodstream - but not procyclic - African trypanosomes, the total cellular concentration of lipoamide dehydrogenase increases with increasing cell densities. In procyclic parasites, lipoamide dehydrogenasemRNA depletion causes an even stronger proliferation defect that is not reversed by presence of thymidine
physiological function
dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD. Since this reaction is the final step of a series of catalytic reaction of pyruvate dehydrogenase multi-enzyme complex (PDC), LipDH is a key enzyme to maintain the fluent metabolic flow
physiological function
-
dihydrolipoamide dehydrogenase is a component in the pyruvate-, 2-oxooglutarate- and branched-chain oxoacid dehydrogenase complexes and in the glycine cleavage system
physiological function
dihydrolipoamide dehydrogenase is the E3 subunit of the mitochondrial pyruvate dehydrogenase complex, rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3
physiological function
-
dihydrolipoamide dehydrogenase of Escherichia coli is a bacterial enzyme that is involved in the central metabolism and shared in common between the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. The presence of oligomeric forms of the enzyme is determined by the multifunctionality of LpD in the cell, in particular, the required stoichiometry in the complexes. The E3 enzyme activity is essential for aerobic respiration. Dihydrolipoamide dehydrogenase plays an equally important role in anaerobic organisms, since this enzyme is involved in the synthesis of branched-chain keto and amino acids
physiological function
E3 catalyzes the reoxidation of the dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of these dehydrogenase complexes
physiological function
E3 is an essential component in pyruvate, 2-oxoglutarate and branched-chain 2-oxo acid dehydrogenase complexes. E3 catalyzes the reoxidation of a dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of the three 2-oxo acid dehydrogenase complexes
physiological function
human dihydrolipoamide dehydrogenase is a flavoenzyme component (E3) of the human 2-oxoglutarate dehydrogenase complex and few other dehydrogenase complexes
physiological function
in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview
physiological function
in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview
physiological function
in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview
physiological function
LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase
physiological function
-
pyruvate dehydrogenase complex, PDC, is a multi-enzyme complex comprising an E1, pyruvate decarboxylase, an E2, dihydrolipomide acetyltransferase, and an E3, dihydrolipoamide dehydrogenase. Plasmodium PDC is essential for parasite survival in the mosquito vector and for late liver stage development in the human host
physiological function
the enzyme DLDH shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of hDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations. Native DLDH is tethered to the pyruvate dehydrogenase complex by interactions with a mediatory protein, E3 binding protein (E3BP), via a region that overlaps with the putative TiO2?binding site, involving V347, H348, D413, E437, Y438, G439, E443, D444, and R447
physiological function
-
the enzyme shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of rhDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations
physiological function
the enzyme, as the E3 component of the pyruvate decarboxylase complex, has reactive oxygen species generating activity
physiological function
-
the enzyme is involved in adhesion to polystyrene as well as coelomocytes and other tissues like body wall, tentacle, muscle, respiratory tree and intestine from sea cucumber Apostichopus japonicas
physiological function
-
the enzyme regulates cystine deprivation-induced ferroptosis in head and neck cancer
physiological function
-
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
-
physiological function
-
LPD is a useful biocatalyst for regenerating NAD+
-
physiological function
Starkeyomyces koorchalomoides FDUS 0337
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
-
physiological function
-
the enzyme is involved in adhesion to polystyrene as well as coelomocytes and other tissues like body wall, tentacle, muscle, respiratory tree and intestine from sea cucumber Apostichopus japonicas
-
physiological function
-
the enzyme shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of rhDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations
-
physiological function
-
LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase
-
physiological function
-
dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
-
additional information
-
a homology model for PfaE3 reveals an extra anti-parallel beta-strand at the position where human E3BP (E3-binding protein) interacts with E3, a parasite-specific feature that may be exploitable for drug discovery against PDC. E3 enzyme homology structure modelling using the human enzyme structure, PDB ID 2F5Z
additional information
-
all of the E3 enzymes function as dimers, and their active site contains the reactive disulfide bridge, which is directly involved in catalysis
additional information
conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity
additional information
location of residue Cys50 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
location of residue H329 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
location of residues Pro156 and Pro303 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis thaliana
additional information
-
mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis thaliana
additional information
-
molecular dynamics simulation the conformation of enzyme LADH that is proposed to be compatible with the reactive oxygen species (ROS) generation
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
residue Ala328 is absolutely conserved, suggesting that it might be important for the structure and function of human E3. Ala328 is a component of alpha-helix 8 and is located near the presumed dihydrolipoamide binding channel. Ala328 is also located close to the active disulfide center between Cys45 and Cys50
additional information
-
structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template
additional information
-
structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template
-
additional information
-
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
-
additional information
-
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
-
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tetramer
present at pH 5.8 and 7.5, active at pH 7.5
trimer
-
gel filtration, 3 * 28000 Da
?
-
x * 28206, sequence analysis
?
-
x * 63489, calculated
?
-
x * 63489, calculated
-
?
x * 54000, about, sequence calculation, x * 55000, SDS-PAGE
?
-
x * 51274, calculation from nucleotide sequence
?
-
x * 66500, SDS-PAGE
-
?
-
x * 99000, MBP-tagged enzyme, SDS-PAGE
?
-
x * 28430, sequence analysis
?
-
x * 49342, electrospray mass spectrometry
?
-
x * 56000, mitochondrial enzyme, SDS-PAGE
?
-
x * 49757, mitochondrial enzyme, electrospray mass spectrometry
?
-
x * 52000, enzyme from chloroplast, SDS-PAGE
?
-
x * 52614, enzyme from chloroplast, electrospray mass spectrometry
?
x * 57000, SDS-PAGE, His-tagged recombinant protein
?
-
x * 57000, SDS-PAGE, His-tagged recombinant protein
-
?
-
x * 58000, enzyme from heart, SDS-PAGE
?
-
x * 56000, enzyme from liver enzyme
?
-
x * 49690, calculation from nucleotide sequence
?
-
x * 50900, isoform DLD1, calculated from amino acid sequence
?
-
x * 51000, isoform DLD1, SDS-PAGE
?
-
x * 53000, isoform DLD2, SDS-PAGE
?
-
x * 53160, isoform DLD2, calculated from amino acid sequence
?
-
x * 50900, isoform DLD1, calculated from amino acid sequence
-
?
-
x * 51000, isoform DLD1, SDS-PAGE
-
?
-
x * 53000, isoform DLD2, SDS-PAGE
-
?
-
x * 53160, isoform DLD2, calculated from amino acid sequence
-
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
2 * 50000, SDS-PAGE, 2 * 53000, sequence analysis
dimer
-
2 * 56000, SDS-PAGE
dimer
-
x * 46000, SDS-PAGE
dimer
x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 50216, amino acid sequence calculation
dimer
molecular sieving HPLC
dimer
wild-type and mutants, molecular sieving HPLC
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 55000, about, SDS-PAGE
dimer
2 * 52000, present at pH 5.8 and 7.5, active at pH 7.5
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
homodimer
2 * 45400, sequence analysis, 2 * 45000, SDS-PAGE
homodimer
-
2 * 50000, SDS-PAGE
homodimer
2 * 50000, SDS-PAGE
homodimer
2 * 55000, SDS-PAGE
homodimer
-
2 * 54000, SDS-PAGE
homodimer
-
x-ray crystallography
homodimer
2 * 50216, sequence calculation
homodimer
homodimeric structure model of human E3, PDB ID for 1ZMC
homodimer
2 * 50216, calculated from amino acid sequence
homodimer
-
2 * 50600, variant 2, SDS-PAGE
homodimer
-
2 * 56300, variant 1, SDS-PAGE
homodimer
-
2 * 50600, variant 2, SDS-PAGE
-
homodimer
-
2 * 56300, variant 1, SDS-PAGE
-
homodimer
2 * 50000, SDS-PAGE
homodimer
2 * 49912, calculated from amino acid sequence
homodimer
-
2 * 50000, SDS-PAGE
-
homodimer
-
2 * 49912, calculated from amino acid sequence
-
homodimer
-
2 * 64000, recombinant Hs-tagged enzyme, SDS-PAGE
monomer
-
1 * 50000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 * 50000, recombinant His-tagged enzyme, SDS-PAGE
-
monomer
1 * 54000, only present and active at pH 5.8
additional information
-
in solution LpD exists as an equilibrium mixture of a dimer and a tetramer, small-angle X-ray scattering and analytical ultracentrifugation
additional information
-
the homodimeric enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
additional information
the enzyme is the E3 component of 2-keto acid dehydrogenase multienzyme complex
additional information
-
the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions
additional information
-
-
additional information
-
EC 1.8.1.4 is the E3-protein component of the mitochondrial 2-oxoacid dehydrogenase multienzyme complexes and the L-protein component of the glycine decarboxylase system
additional information
-
2 distinct dihydrolipoamide dehydrogenases, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
additional information
-
E3 enzyme homology structure modelling using the human enzyme structure, PDB ID 2F5Z
additional information
-
structure homology modeling of rhDLDH
additional information
-
structure homology modeling of rhDLDH
-
additional information
-
dihydrolipoamide dehydrogenase E3 is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, wheras it is bound to the pyruvate dehydrogenase complex through a protein X
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C44S
-
0.003% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature
C49S
-
0.012% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature
K53R
-
spectral and redox properties of FAD in the mutant enzyme as well as the interaction of the flavin with bound NAD+ are profoundly affected by the mutation, K53R does not catalyze either the dihydrolipoamide-NAD+ or the NADH-lipoamide reactions except at very low concentrations of reducing substrate. The absorbance spectrum in the visible and near-ultraviolet is little changed from that of wild-type enzyme, in contrast to wild-type enzyme the spectrum of K53R is sensitive to pH. Unlike the wild-type enzyme, the binding of beta-NAD+ to K53R alters the spectrum
E354K
-
is significantly less sensitive to NADH inhibition than the native LPD
H322Y
-
upon purification LPD loses activity and associated FAD at the gel filtration step
E423A
in 2 M KCl, the mutant is significantly less active than wild-type, decreased Km value for dihydrolipoamide. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423D
wild-type and E423D mutant enzyme are much less active in the absence of KCl than in its presence. The mutant enzyme is inactivated at temperatures around 20°C lower than the wild-type
E423Q
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423S
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423A
-
in 2 M KCl, the mutant is significantly less active than wild-type, decreased Km value for dihydrolipoamide. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
-
E423D
-
wild-type and E423D mutant enzyme are much less active in the absence of KCl than in its presence. The mutant enzyme is inactivated at temperatures around 20°C lower than the wild-type
-
E423Q
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
-
E423S
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
-
A1444G
-
substitution located in exon 13 leading to 20% of wild type activity
A328V
site-directed mutagenesis of the conserved residue, the site-specific dihydrolipoamide dehydrogenase mutant shows a switched kinetic mechanism, it shows a random sequential kinetic mechanism with an interaction factor (alpha) of 8.5. The mutation deteriorates substantially the catalytic power of human E3 enzyme increasing the binding affinity for NAD+ and dihydrolipoamide . The mutation triggers this potential intrinsic property of the enzyme causing the kinetic mechanism of the mutant to switch from a ping-pong mechanism to a random sequential mechanism
C45S
-
Ser-45 mutant is highly purified, shows 5270fold lower activity than wild-type enzyme. Destroyed disulfide bond between Cys-45 and Cys-50 of the active disulfide center in human E3. UV-visible spectrum of the Ser-45 mutant is similar to that of the reduced form of the enzyme and the second fluorescence emission of the mutant disappears
C45Y
-
purification of the Tyr-45 mutant is not successful. Recombinant human E3 becomes too unstable to be easily obtained from Escherichia coli
C50A
site-directed mutagenesis, catalytic efficiency of mutant C50A toward NAD+ decreases 5317fold compared to the wild-type enzyme, the mutation destroys the active disulfide center between Cys45 and Cys50, which restricts the freedom of Cys50
C50T
site-directed mutagenesis, catalytic efficiency of mutant C50A toward NAD+ decreases 2057fold compared to the wild-type enzyme, the mutation destroys the active disulfide center between Cys45 and Cys50, which restricts the freedom of Cys50
D413N
-
the mutant shows 119% activity in the forward reaction and 96% activity in the reverse reaction compared to the wild type enzyme
D473L
-
site-directed mutagenesis, mutant shows about 37fold decreased activity and small conformational changes compared to the wild-type enzyme
DELTAG101
naturally occuring mutation, the mutation is involved in E3 deficiency
E192Q
-
specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced
E431A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
E457Q
-
molar ratio of FAD to enzyme is 0.9 compared to 1 for the wild-type enzyme, mutation affects the environment surrounding FAD, decrease in efficiency of electron transfer from the reduced flavin to the oxidized substrate
G426E
naturally occuring mutation, the mutation is involved in E3 deficiency
H329A
site-directed mutagenesis, the kcat value of the mutant is significantly decreased by 24fold as compared to the wild-type, indicating that the mutation severely deteriorates the catalytic power of the enzyme
H348A
-
the mutant shows 60% activity in the forward reaction and 66% activity in the reverse reaction compared to the wild type enzyme
H348L
-
the mutant shows 65% activity in the forward reaction and 74% activity in the reverse reaction compared to the wild type enzyme
H450A
-
shows an increase in proteolytic activity as compared with the wild-type
H452Q
-
molar ratio of FAD to enzyme is 0.94 compared to 1 for the wild-type enzyme, no production of NADH when the enzyme is reduced by dihydrolipoamide, transfer of electrons from the substrate dihydrolipoamide to NAD+ is extremely low
I12T
naturally occuring mutation, the mutation is involved in E3 deficiency
I318T
naturally occuring mutation, the substitution triggers major structural disturbance only at the C-terminus
I358T
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
I51A
-
mutant with about 100fold reduced activity compared to the wild type enzyme
K54E
-
about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-value for lipoamide is increased by about twofold
L99A
the mutation deteriorates the catalytic power of the enzyme substantially
P154A
the mutation makes enzyme binding to both dihydrolipoamide and NAD+ inefficient
P156A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P303A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P325A
-
mutation of highly conserved resdue in the central domain, about 150fold decrease in kcat value
P355A
the mutation makes enzyme binding to NAD+ substantially less efficient. The catalytic efficiency of the mutant toward NAD+ is decreased by 81% compared to the wild type enzyme
P387A
the mutation deteriorates severely the catalytic power of the enzyme
P423A
the mutation makes enzyme binding to both dihydrolipoamide and NAD+ inefficient
P453V
-
1650fold lower specific activity compared to the wild type enzyme
R281K
specific activity is 11.93% to that of wild-type E3. FAD-content is about 93% that of wild-type E3. Kcat of forward reaction is decreased dramatically. Substitution has no effect in the self-dimerization
R281N
specific activity is 12.50% to that of wild-type E3. FAD-content is about 96% that of wild-type E3. Kcat of forward reaction is decreased dramatically. Substitution has no effect in the self-dimerization
R447A
-
the mutant shows 110% activity in the forward reaction and 122% activity in the reverse reaction compared to the wild type enzyme
S456A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
S456A/D444V
-
low levels of residual activity
S53K/K54S
-
about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced. The catalytic rate constant, turnover number/Km, is significantly lower than wild-type
T148G
specific activity is 76.34% to that of wild-type E3. FAD-content is about 710% that of wild-type E3. Substitution has no effect in the self-dimerization
T148S
specific activity is 88.62% to that of wild-type E3. FAD-content is about 92% that of wild-type E3. Substitution has no effect in the self-dimerization
T44V
-
site-directed mutagenesis, mutation of Thr44 of the FAD-binding region to Val, corresponding to the prokaryotic sequence, results in 2.2fold reduced activity with a slightly different microenvironment at the FAD-binding site
W366A
-
mutation of highly conserved residue. kinetic parameters similar to wild-type
Y438F
-
the mutant shows 100% activity in the forward reaction and 112% activity in the reverse reaction compared to the wild type enzyme
A48I
-
the mutation decreases the Km for dihydrolipoamide substrate by 3fold compared to the wild type enzyme
A54I
-
the mutation increases the Km for dihydrolipoamide substrate by 1fold and NAD+ by 3fold compared to the wild type enzyme
C15T
-
the mutation increases the Km for dihydrolipoamide substrate by 5fold and NAD+ by 3fold compared to the wild type enzyme
C38G
-
the mutation increases the Km for NAD+ by 9fold without affecting Km for dihydrolipoamide compared to the wild type enzyme
Cys38Gly
-
the substitution does not show any change in Km value for dihydrolipoamide compared to the wild type enzyme
D49G
-
the mutation decreases the Km for dihydrolipoamide substrate by 2fold compared to the wild type enzyme
A181V
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
A290R
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
D5A
4.3% activity of the wild type enzyme
E91A
49.6% activity of the wild type enzyme
E91K
62.5% activity of the wild type enzyme
F269R
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
F464A
5% activity of the wild type enzyme
G312A/L313G/L314P/Q315M
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
H386A
20% activity of the wild type enzyme
H386K
9% activity of the wild type enzyme
H460E
69.4% activity of the wild type enzyme
H98A
3.3% activity of the wild type enzyme
K103E
17.7% activity of the wild type enzyme
K105A
44.7% activity of the wild type enzyme
K216A
58.3% activity of the wild type enzyme
K220A
81.2% activity of the wild type enzyme
K223A
67.1% activity of the wild type enzyme
K223E
70.5% activity of the wild type enzyme
K224A
55.2% activity of the wild type enzyme
K376A
52.2% activity of the wild type enzyme
K67A
67.3% activity of the wild type enzyme
K67E
64.3% activity of the wild type enzyme
K88E
74.8% activity of the wild type enzyme
L314P
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
N209V
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
N43A
11% activity of the wild type enzyme
R147T
the mutant is more sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
R347S
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
R93A
6.5% activity of the wild type enzyme
R93E
3.6% activity of the wild type enzyme
A181V
-
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
-
A290R
-
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
-
F269R
-
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
-
N209V
-
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
-
R147T
-
the mutant is more sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
-
E91A
-
49.6% activity of the wild type enzyme
-
K220A
-
81.2% activity of the wild type enzyme
-
K223A
-
67.1% activity of the wild type enzyme
-
K224A
-
55.2% activity of the wild type enzyme
-
K67A
-
67.3% activity of the wild type enzyme
-
I192G
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
V191Y
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
I192G
-
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
-
V191Y
-
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
-
K43A
-
unable to express the mutant protein
K43R
-
expresses well, but still has lipoic acid attached
D320N
48.60% specific activity of the wild type enzyme, 82.7% of FAD content compared to that of the wild-type enzyme
D320N
specific activity is 48.6% to that of the wild-type E3. About 82.7% of FAD content compared to that of wild-type E3. Forms the dimer
D413A
-
the mutant shows 85% activity in the forward reaction and 79% activity in the reverse reaction compared to the wild type enzyme
D413A
substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 18%. The binding affinities of the mutant to the di-domain of the E3-binding protein are severely reduced
D444V
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 12% of that of the wild type enzyme
D444V
-
pathogenic mutation, diminishing the ability of E3 to homodimerize
D444V
-
shows weak proteolytic activity with mature frataxin substrate, but consistently cleaves mature frataxin to denoted frataxin products with faster kinetics than the wild-type
D444V
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells
D444V
-
the mutation causes microcephaly, blindness, deafness, mild hypertrophic cardiomyopathy, and metabolic acidosis. The substitution leads to compromised enzyme activity (15% of the control)
E340K
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 38% of that of the wild type enzyme
E340K
-
pathogenic mutation, diminishing the ability of E3 to homodimerize
E340K
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells. The mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
G194C
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
G194C
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells
I445M
naturally occuring mutation, mutant enzyme structure analysis
I445M
naturally occuring mutation, the mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
K37E
-
molar ratio of FAD to enzyme is 0.76 compared to 1 for the wild-type enzyme
K37E
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
M326V
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
M326V
naturally occuring mutation, the mutation is involved in E3 deficiency
N286D
30.84% specific activity of the wild type enzyme, 96% of FAD content compared to that of the wild-type enzyme
N286D
specific activity is 30.84% to that of the wild-type E3. About 96.0% of FAD content compared to that of wild-type E3. Forms the dimer
N286Q
24.57% specific activity of the wild type enzyme, 99.4% of FAD content compared to that of the wild-type enzyme
N286Q
specific activity is 24.57% to that of the wild-type E3. About 99.4% of FAD content compared to that of wild-type E3. Forms the dimer
P453L
-
causes E3 deficiency
P453L
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells. The mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
R447G
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 28% of that of the wild type enzyme
R447G
naturally occuring mutation, the mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
R460G
-
missense mutation, the dissociation constant is three orders of magnitude higher than that of wild-type E3
R460G
-
pathogenic mutation, diminishing the ability of E3 to homodimerize
Y438A
-
the mutant shows 100% activity in the forward reaction and 91% activity in the reverse reaction compared to the wild type enzyme
Y438A
substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 9%. The binding affinities of the mutant to the di-domain of the E3-binding protein are severely reduced and binding of is accompanied by an unfavorable enthalpy change and a large positive entropy change
Y438H
-
the mutant shows 99% activity in the forward reaction and 92% activity in the reverse reaction compared to the wild type enzyme
Y438H
substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 20%. The binding affinities of the mutant to the di-domain of the E3-binding protein ire severely reduced
additional information
generation of DLDH2 enzyme knockout mutant plants, the aos phenotype in mtlpd2-2 is due to disruption of mtLPD2. Mutation of mtLPD2 enhances As(V)-induced changes in metabolite pools, aos phenotype analysis, overview
additional information
-
generation of DLDH2 enzyme knockout mutant plants, the aos phenotype in mtlpd2-2 is due to disruption of mtLPD2. Mutation of mtLPD2 enhances As(V)-induced changes in metabolite pools, aos phenotype analysis, overview
additional information
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deletion mutant DELTAG101 causes E3 deficiency
additional information
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insertion mutant Mg7 has an insertion site between amino acids 222 and 223, preventing the expression of over 50% of the carboxyl-terminal portion of the 467-amino-acid protein, the mutant is classified as a potential virulence mutant
additional information
-
generation of Pfae3 deletion mutants of Plasmodium falciparum, the gene is replaced by the selectable marker hdhfr after initial positive selection with WR99210 followed by negative selection using 5-fluorocytosine generating the line 3D7DELTAae3, phenotype, overview
additional information
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deletion of the LPD1 gene prevents oxidative stress in npt1DELTA and bna6DELTA mutants
additional information
-
protein expressed without lipoic acid is indistinguishable from the wild-type protein. The protein without a lipoyl protein domain has a 2-3fold higher turnover number, a lower Ki for NADH, and a higher Ki for lipoamide compared with the other two enzymes
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bfmBC gene encoding DLD. Ligated into vector pCR2.1, and introduced into Escherichia coli DH5alpha. Insert DNA recovered from the recombinant plasmid ligated into vector pET-28a(+), yielding pET-bfmBC and expressed in Escherichia coli BL21 (DE3)
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex, expression in Escherichia coli
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DNA and amino acid sequence determination and analysis of both lipdh genes using RT-PCR, expression of the mitochondrial isozyme as GFP-fusion protein giving green fluorescence and of the apicoplast isozyme fused to acyl-carrier-protein resulting in red fluorescence, expression of truncated mitochondrial and apicoplastic isozymes lacking the putative target sequences as His-tagged proteins in Escherichia coli strain BL21-RIL(DE3), the apicoplast isozyme is expressed at very low levels
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DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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expressed in Escherichia coli
expressed in Escherichia coli as a recombinant protein
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Codon Plus RLI cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli JM83 cells
expressed in Escherichia coli M109(lambdaDE3)
-
expressed in Escherichia coli M15 cells
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expressed in Escherichia coli M15pREP4 cells
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expressed in Escherichia coli Rosetta-gami (DE3) cells
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expressed in Escherichia coli Rosetta-gami cells
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expressed in Escherichia coli strain JRG 1342
-
expressed in Escherichia coli using the cytoplasmic expression vectors, pET3a and pET3d. Expressed as inclusion bodies and refolded by solubilisation in 8 M urea followed by dilution into a buffer containing 2 M KCl, 0.010 mM FAD, 1 mM NAD+, and 0.3 mM GSSG/3 mM GSH
expressed in Escherichia coli XL1-Blue
-
expression in a strain of Haloferax volcanii lacking dihydrolipoamide dehydrogenase activity
expression in Escherichia coli
expression in Escherichia coli or in Corynebacterium glutamicum, the cloned gene is expressed in Corynebacterium glutamicum cells harbouring the gene on a plasmid shows 12fold higher specific LPD activity when compared to the wild-type strain
expression in Escherichia coli strain JRG 1342
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expression of D473L mutant in Escherichia coli strain XL1-Blue
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expression of mutant T44V in Escherichia coli strain XL1-Blue
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gene dld, DNA and amino acid sequence determination and analysis, genotyping
gene dld, located on chromosome 7, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL-1 Blue
gene dld, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha
gene dld, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL-1 Blue
gene DLD, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene encoding hDLDH but excluding the N-terminal 1?35 signal peptide region and containing an N-terminal His6-tag, recombinant expression in Escherichia coli strain BL21(DE3)
gene lpd, recombinant expression in Escherichia coli strain BL21(DE3)
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gene lpd2, recombinant expression of GUS-linked enzyme in Arabidopsis thaliana ecotype Col-0 in cotyledons, rosette leaves and roots (in the cap of the established lateral roots, but not in the cap of the main roots) via transformation by Agrobacterium tumefaciens strain GV3101
gene lpd3, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene lpdG, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene lpdV, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Pfae3, recombinant expression of His-tagged enzyme in Escherichia coli strain NovaBlue (DE3), transfection of pCC1-Pfae3 Plasmodium falciparum 3D7 erythrocytic stages
-
His-tagged wild-type and mutant proteins overexpressed in Escherichia coli
into vector pET101/D TOPO and expressed in Escherichia coli BL21(DE3)
-
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
mutants cloned into pQE-9 vector
Mycobacterium smegmatis over-expressing LpdC protein
-
overexpressed in the parent organism by using the halophilic archaeal rRNA promoter
overexpression in Escherichia coli
recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strain BL21(DE3)
wild-type and mutant enzymes K37E, H452Q and E457Q
-
wild-type and mutant enzymes K37E, H452Q and E457Q, overexpression in Escherichia coli
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wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q, overexpression in Escherichia coli
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wild-type DLD and mutant D444V expressed in Escherichia coli BL21 with an N-terminal six-histidine tag. C-term DLD, the interface domain residing the proteolytic activity of DLD, expressed in Escherichia coli without any tags
-
-
-
expressed in Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli
Starkeyomyces koorchalomoides
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
-
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
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analysis
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development of a blue native-PAGE-based method for isolation of enzymatically active DLDH from animal tissues and visualization as well as quantification of its diaphorase activity using the NADH/nitroblue tetrazolium detection system
drug development
-
a homology model for PfaE3 reveals an extra anti-parallel beta-strand at the position where human E3BP (E3-binding protein) interacts with E3, a parasite-specific feature that may be exploitable for drug discovery against pyruvate dehydrogenase complex, PDC. Plasmodium PDC is essential for parasite survival in the mosquito vector and for late liver stage development in the human host, suggesting its suitability as a target for intervention strategies against malaria
degradation
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conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme
degradation
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decreased activity of DLDH induced by valproic acid metabolites may, at least in part, account for the impaired rate of oxygen consumption and ATP synthesis in mitochondria if 2-oxoglutarate or glutamate are used as respiratory substrates, thus limiting the flux of these substrates through the citric acid cycle
degradation
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DLD is required for hamster acrosome reaction
degradation
N286 and D320 play a role in the catalytic function of the E3
degradation
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S456 and E431 form a catalytic dyad in the DLD monomer, whereas H450, by forming a hydrogen bond with E431, may decrease the ability of E431 to polarize the hydroxyl group of S456
degradation
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shows flavin reductase activity with moderate diaphorase activity
degradation
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shows NADH-dependent tellurite reductase activity in vitro
degradation
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shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
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shows strong diaphorase activity
degradation
T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3
diagnostics
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Bacillus sphaericus DLD-diaphorase exhibits considerable potential to be used as a component of diagnostic tests for the quantification of metabolites
diagnostics
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Bacillus sphaericus DLD-diaphorase exhibits considerable potential to be used as a component of diagnostic tests for the quantification of metabolites
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medicine
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mutations of the enzyme cause the often-fatal human disease known as E3 deficiency
medicine
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brain DLDH expression and activity undergo independent postnatal maturational increases. Senescence does not confer any detectable change in the activity of DLDH or its susceptibility to inactivation by mitochondrial oxidative stress
medicine
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dihydrolipoyl dehydrogenase is an important source of reactive oxygen species leading to life span limitation
medicine
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direct involvement of LpdC in the prolonged retention of coronin-1 on the phagosome, thus promoting phagosome maturation arrest. Under the influence of IFNgamma, LRG-47 is recruited to the phagosome and mediates dislocation of coronin-1 leading ultimately to phagosome acidification and recruitment of lysosomal vacuoles and phagolyosome fusion
medicine
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direct involvement of LpdC in the prolonged retention of coronin-1 on the phagosome, thus promoting phagosome maturation arrest. Under the influence of IFNgamma, LRG-47 is recruited to the phagosome and mediates dislocation of coronin-1 leading ultimately to phagosome acidification and recruitment of lysosomal vacuoles and phagolyosome fusion
medicine
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linkage and association analysis of diplotypes in the DLD gene with Alzheimer's from the National Institute of Mental Health-National Cell Repository for Alzheimer's disease and Italian data series, controlling for Gender and ApoE e4 status. Significant evidence of association of DLD with Alzheimer's disease. Combining the linkage and association study results for DLD together, leads to a p-value that is more significant than any of the individual p-value results for DLD. Only with sufficiently large sample sizes it is possible to rule out whether the DLD gene is in fact associated with Alzheimers disease
medicine
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lipoamide dehydrogenase activity and metallothionein levels may be critical for dopaminergic neuronal survival in Parkinson's disease. 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine can affect the lipoamide dehydrogenase activity and metallothionein content to exert its neurotoxicity
medicine
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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
medicine
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
medicine
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due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues
medicine
due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues
medicine
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Arg-Gly-Asp-modified enzyme enhances the adhesion of bone forming cells to titanium dioxide implant surfaces
medicine
the enzyme is a DNA chelating agent. Enzyme binding to DNA presents a moonlight activity which may be used for DNA alkylating in cancer treatment
medicine
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lipoamide dehydrogenase activity and metallothionein levels may be critical for dopaminergic neuronal survival in Parkinson's disease. 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine can affect the lipoamide dehydrogenase activity and metallothionein content to exert its neurotoxicity
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medicine
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enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
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medicine
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due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues
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additional information
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a mutation in LPD leads to a pyruvate dehydrogenase complex that is less sensitive to inhibition by NADH, allowing the enzyme to function in an anaerobic culture, which changes the fermentation profile of the mutant. Presence and functional activity of such an NADH-insensitive pyruvate dehydrogenase may have significant unexplored physiological and biotechnological applications
additional information
high stability of rBfmBC may make it useful for practical use
additional information
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high stability of rBfmBC may make it useful for practical use
additional information
metabolic context(s) of DLDHs remains an open question
additional information
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metabolic context(s) of DLDHs remains an open question
additional information
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the lipoyl protein domain (but not lipoic acid alone) plays a regulatory role in the enzymatic characteristics of pneumococcal DLDH