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Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
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1.8.1.4 dihydrolipoyl dehydrogenaseIUBMB Comments
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein .
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Word Map
- 1.8.1.4
-
multienzyme
- fad
- acetyltransferase
- dehydrogenases
- alpha-ketoglutarate
- flavin
- flavoproteins
-
branched-chain
- transacetylase
-
azotobacter
- vinelandii
-
subcomplexes
- thiamin
-
alpha-keto
- acidosis
-
mercuric
- alpha-ketoacids
-
flavoenzymes
- succinyltransferase
- 2-oxoacids
- trypanothione
- friedreich
-
1.2.4.1
-
radiofrequency
-
subunit-binding
-
ashkenazi
- h-proteins
-
myenteric
- degradation
- medicine
- diagnostics
- analysis
- drug development
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
lipoamide dehydrogenase, dihydrolipoamide dehydrogenase, dldh, l-protein, dihydrolipoyl dehydrogenase, nadh diaphorase, lipdh, e3 component, hladh, lipoyl dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CIP50
coronin-interacting protein
DHLipDH
diaphorase
dihydrolipoamide dehydrogenase
dihydrolipoamide dehydrogenase E3
dihydrolipoamide:NAD+ oxidoreductase
DLD
DLDH
DLDH2
E3
LAD
LADH
LDH
LipDH
lipoamide dehydrogenase
lipoamide dehydrogenase C
lipoamide-dehydrogenase-valine
lipoyl dehydrogenase
LPD
LPD1
LPD2
Lpd3
LpdA
LpdC
LpdG
LpdV
NAD(P)H:lipoamide oxidoreductase
NADH dehydrogenase
NADH diaphorase
NADH:lipoamide oxidoreductase
pdhL
rhDLDH
TAase
additional information
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
E3
-
pyruvate dehydrogenase complex is composed of multiple copies of three catalytic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3)
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
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
LPD1
-
plastidial LPD1 encodes one of the two E3 isoforms found in the plastidial pyruvate dehydrogenase complex
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
-
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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
involvement of a reversibly reducible disulfide bond in catalytic mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
Asp473 is important for efficient catalytic function of the enzyme
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
formation of a FADH2-NAD+ intermediate in catalysis, reaction mechanism of reductive and oxidative half-reactions involving enzyme, FAD/FADH2, and NAD+/NADH
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron-reduced enzyme, both redox centers are reduced, mechanism of the diaphorase reaction which occurs when the enzyme is in the four-electron-reduced state
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
the mitochondrial isozyme shows ping pong kinetic mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Ddihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Dihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Dihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
kinetic mechanism of human E3 enzyme is a ping-pong mechanism. In human E3, dihydrolipoamide binds to the si-face of FAD, whereas NAD+ binds to the re-face. These two spatially separate substrate binding sites can allow the enzyme to form a ternary complex with two substrates, which is an essential feature of the sequential mechanism
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
-
catalyzes reoxidation of reduced lipoate attached to H-protein, a lipoic acid-containing protein
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Biosynthesis of secondary metabolites, Citrate cycle (TCA cycle), Glycine, serine and threonine metabolism, Glycolysis / Gluconeogenesis, Lysine degradation, Microbial metabolism in diverse environments, Propanoate metabolism, Pyruvate metabolism, Tryptophan metabolism, Valine, leucine and isoleucine degradation
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SYSTEMATIC NAME
IUBMB Comments
protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [6].
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CAS REGISTRY NUMBER
COMMENTARY
9001-18-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-dimethoxy-1,4-benzoquinone + NADH
? + NAD+
8.0% activity compared to lipoamide
-
?
2-hydroxy-1,4-benzoquinone + NADH
2-hydroxy-1,4-benzoquinol + NAD+
-
-
-
?
2-methyl-1,4-benzoquinone + NADH
2-methyl-1,4-benzoquinol + 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
-
?
benzyl viologen + NADH
? + NAD+
-
2.9% of the activity with lipoamide
-
?
DL-lipoylpentanoate + NADH
? + NAD+
-
100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state
-
?
ferrocene + NADH
? + NAD+
3.6% activity compared to lipoamide
-
?
ferrocenecarboxylic acid + NADH
? + NAD+
4.1% activity compared to lipoamide
-
?
iodonitrotetrazolium chloride + NADH
? + NAD+
19.3% activity compared to lipoamide
-
?
lipoamide + 3-acetylpyridine adenine dinucleotide
dihydrolipoamide + ?
-
-
-
?
lipoamide + nicotinamide hypoxanthine dinucleotide
dihydrolipoamide + ?
-
-
-
?
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
-
-
-
?
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
-
?
nitrotetrazolium blue + NADH
? + NAD+
2.9% activity compared to lipoamide
-
?
nitrotetrazolium blue + NADH + H+
reduced nitrotetrazolium blue + NAD+
-
-
-
r
pyocyanin + NADH + H
reduced pyocyanin + NAD+
pyocyanin is reported to stimulate respiration
-
?
reduced DL-lipoamide + NAD+
oxidized DL-lipoamide + NADH
-
-
-
r
resazurin + NADH
? + NAD+
155.8% activity compared to lipoamide
-
?
resorufin + NADH
? + NAD+
19.1% activity compared to lipoamide
-
?
sulfonated tetrazolium WST-1 + NADH
formazan derivative + NAD+
39.2% activity compared to lipoamide
-
?
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+
-
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+
-
-
?
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
-
-
-
?
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-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
-
-
-
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
?
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+
-
-
?
dihydrolipoamide + NAD
lipoamide + NADH + H+
dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
DLDH activity, forward reaction
-
r
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
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
?
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
-
alternate oxidation and reduction of an intrachain disulfide bond
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
specific substrate
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
specific substrate
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
NADH:lipoamide oxidoreductase activity, reverse reaction
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
100% activity
-
?
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+
-
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
-
-
-
?
O2 + NADH
?
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
?
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+
-
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+
-
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+
-
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
-
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
thio-NAD+ + NADH
thio-NADH + NAD+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
?
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)+
-
reaction is important to protect the cell e.g. from oxidative stress
-
?
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
-
r
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
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)+
-
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.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD
FAD
-
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
FAD
-
wild-type enzyme contains 1 FAD per subunit, mutant enzyme K37E has about 25% less bound FAD
FAD
-
the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates
FAD
-
tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
-
a flavoprotein, each monomer of 51000 Da binds one molecule of FAD
FAD
a single FAD is non-covalently arranged in each subunit
FAD
one FAD as a prosthetic group at each subunit, binding structure analysis
NAD+
-
-
NAD+
-
-
393971, 393993, 394003, 394004, 659101, 672869, 673943, 674382, 674759, 675350, 677161, 691569, 711099
NAD+
-
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+
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
NADH
-
the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
additional information
-
enzyme contains a redox-active disulfid, the cofactor cycles between reduced and oxidized state during catalysis, in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron.reduced enzyme, both redox centers are reduced
-
additional information
-
enzyme contains a redox-active disulfide, the cofactor cycles between reduced and oxidized state during catalysis
-
additional information
-
contains neither FMN nor FAD in the molecule
-
additional information
FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
-
additional information
-
FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM
Fe
-
amino acid sequence homology indicates the presence of a Fe-containing rubredoxin-like domain. The amount of iron is determined to be 1.1 molecule per rDiaA molecule by ICP atomic emission spectroscopy
Mg2+
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
Zn2+
additional information
Zn2+
-
highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM, Zn2+ slightly elevates the pH-optimum of the enzyme
additional information
1 mM Na+, Ca2+, Mg2+, Mn2+, Fe3+, Zn2+, Pb2+, and Hg2+ do not enhance enzyme activity
additional information
-
1 mM Na+, Ca2+, Mg2+, Mn2+, Fe3+, Zn2+, Pb2+, and Hg2+ do not enhance enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Cd2+
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in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
chlorpromazine
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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
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induces 71% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
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
Fe2+
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at high concentrations has significant inhibitory effect on the lipoamide dehydrogenase activity
fluphenazine
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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
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inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
Guanidine-HCl
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4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible
H2O2
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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)
isobiopterin
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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
p-[(bromoacetyl)-amino]phenyl arsenoxide
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irreversible active site directed inactivation
Pb2+
1 mM shows strong inhibitory effect on recombinant BfmBC activity (more than 80% inhibition)
perphenazine
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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
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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
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when purified DLDH is eluted directly into potassium phosphate buffer, the enzymatic activity rapidly decreases
prochlorperazine
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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
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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
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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
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0.1 mM, 40% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4
propionylpromazine
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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
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induces a 62% loss in diaphorase activity at 2 mM and an 88% loss at 10 mM
S-nitrosoglutathione
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induces 84% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
thioridazine
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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
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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
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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
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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-dephosphoCoA
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uncompetitive inhibitor, 0.5-1.0 mM inhibit DLDH activity