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coronin-interacting protein
dehydrogenase, lipoamide
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-
-
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dehydrolipoate dehydrogenase
-
-
-
-
dihydrolipoamide dehydrogenase
dihydrolipoamide dehydrogenase E3
dihydrolipoamide:NAD+ oxidoreductase
dihydrolipoic dehydrogenase
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-
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-
dihydrolipoyl dehydrogenase
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-
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-
E3 component of 2-oxoglutarate dehydrogenase complex
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E3 component of acetoin cleaving system
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E3 component of alpha keto acid dehydrogenase complexes
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E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
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E3 component of pyruvate complex
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E3 lipoamide dehydrogenase
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E3 protein component of 2-oxoacid dehydrogenase multienzyme complexes
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E3 subunit of the alpha-ketoglutarate dehydrogenase complex
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EC 1.6.4.3
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formerly
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Glycine cleavage system L protein
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Glycine oxidation system L-factor
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lipoamide dehydrogenase (NADH)
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lipoamide dehydrogenase C
lipoamide dehydrogenase2
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lipoamide oxidoreductase (NADH)
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lipoamide reductase
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lipoamide-dehydrogenase-valine
lipoate dehydrogenase
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lipoic acid dehydrogenase
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NAD(P)H:lipoamide oxidoreductase
NADH:lipoamide oxidoreductase
nicotinamide adenine dinucleotide diaphorase
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CIP50

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-
coronin-interacting protein

-
-
coronin-interacting protein
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-
DHLipDH

-
diaphorase

-
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-
dihydrolipoamide dehydrogenase

-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
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dihydrolipoamide dehydrogenase
-
-
658466, 659099, 659101, 672869, 674382, 675350, 677161, 691569, 694356, 694854, 741757
dihydrolipoamide dehydrogenase
-
674943, 693271, 713452, 741807, 741998, 742087, 742221, 743050, 743051, 743052, 743127, 743767
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 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
-
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
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DLD

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DLDH

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DLDH2

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E3

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E3
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pyruvate dehydrogenase complex is composed of multiple copies of three catalytic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3)
LAD

-
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LADH

-
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LADH
Starkeyomyces koorchalomoides
-
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
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LDH

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LipDH

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lipoamide dehydrogenase

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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase
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lipoamide dehydrogenase C

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lipoamide dehydrogenase C
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lipoamide-dehydrogenase-valine

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lipoamide-dehydrogenase-valine
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is the specific E3 subunit for branched-chain keto acid dehydrogenase
lipoamide-dehydrogenase-valine
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is the specific E3 subunit for branched-chain keto acid dehydrogenase
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lipoyl dehydrogenase

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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

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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

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rhDLDH

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TAase

Starkeyomyces koorchalomoides
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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
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additional information

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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
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enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
additional information
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cf. EC 1.6.99.3
additional information
-
cf. EC 1.6.99.3
-
additional information
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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
DL-6,8-thiooctic acid amide + NADH
? + NAD+
-
-
-
-
r
DL-alpha-lipoamide + NADH
dihydrolipoamide + NAD+
-
-
-
-
?
DL-lipoamide + NADH
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-(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+
-
-
-
?, 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
-
-
?
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+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
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
?
-
-
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-phosporylation, 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-(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-phosporylation, 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

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