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Enzyme Nomenclature
Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
for references in articles please use BRENDA:EC1.8.1.4
Word Map on EC 1.8.1.4
- 1.8.1.4
-
multienzyme
- fad
- disulfide
- alpha-ketoglutarate
- flavin
- flavoproteins
-
branched-chain
-
transacetylase
- vinelandii
- thioredoxin
-
azotobacter
- thiamin
-
alpha-keto
-
subcomplexes
- acidosis
-
flavoenzymes
-
alpha-ketoacids
-
mercuric
- 2-oxoacids
-
succinyltransferase
- trypanothione
- friedreich
-
two-electron
-
subunit-binding
- protochlorophyllide
-
t-proteins
-
ashkenazi
-
ketoacids
- medicine
-
frontotemporal
-
fad-binding
- degradation
-
1.2.4.1
- analysis
- diagnostics
- drug development
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.1.4
-
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RECOMMENDED NAME
GeneOntology No.
dihydrolipoyl dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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+
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+
the mitochondrial isozyme shows ping pong kinetic mechanism
-
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+
Asp473 is important for efficient catalytic function of the enzyme
-
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+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
oxidation
-
catalyzes reoxidation of reduced lipoate attached to H-protein, a lipoic acid-containing protein
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3D7, 2 lipdh genes encoding 2 isozymes in mitochondrion and apicoplast, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
-
-
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex
-
-
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex; K-12
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-
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex
-
-
-
393971, 393993, 394003, 394004, 658466, 659099, 659101, 672869, 673943, 674382, 674759, 675350, 677161, 691569, 694356, 694854, 711099, 724686
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
enzyme is inactivated by complex III- but not complex I-derived reactive oxygen species, and the accompanying loss of activity due to the inactivation can be restored by cysteine and glutathione. H2O2 instead of superoxide anion is responsible for the inactivation, and protein sulfenic acid formation is associated with the loss of enzymatic activity
physiological function
malfunction
-
the homozygous deletion mutant lpd1/lpd1 is unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibits a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5 mM of hydrogen peroxide and shows filamentation defects
malfunction
-
enhanced arsenate and arsenite sensitivity is due to the disruption of the plastidial LPD1 and LPD2 genes
malfunction
-
the homozygous deletion mutant lpd1/lpd1 is unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibits a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5 mM of hydrogen peroxide and shows filamentation defects
-
physiological function
-
effects of insulin treatment on HuC/HuD myoenteric neurons, NADH diaphorase, and nNOS-positive myoenteric neurons of the duodenum of adult rats with acute diabetes is investigated: The density of NADH diaphorase-positive neurons in animals from the diabetic group and in the insulin treated diabetic group is greater than in the control group, indicating that short-term diabetes increases the activity of respiratory chain enzymes
physiological function
Starkeyomyces koorchalomoides
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
physiological function
-
dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
physiological function
LPD is a useful biocatalyst for regenerating NAD+
physiological function
-
plastidial LPD expression quantitatively controls Arabidopsis arsenate sensitivity
physiological function
-
dihydrolipoamide dehydrogenase is a FAD-linked subunit of 2-oxooglutarate, pyruvate and branched-chain amino acid dehydrogenases and the glycine cleavage system, transfering electrons from the dihydrolipoic acid prosthetic group to the NAD+ cofactor via its FAD center
physiological function
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lipoamide dehydrogenase-deficient Mycobacterium tuberculosis is severely attenuated in wild type and immunodeficient mice. When dihydrolipoamide acyltransferase is absent, Mycobacterium tuberculosis upregulates an lipoamide dehydrogenase-dependent branched chain keto-acid dehydrogenase encoded by pdhA, pdhB, pdhC and lpdC. Without lipoamide dehydrogenase, Mycobacterium tuberculosis cannot metabolize branched chain amino acids and potentially toxic branched chain intermediates accumulate. Mycobacterium tuberculosis deficient in both dihydrolipoamide acyltransferase and pdhC phenocopies lipoamide Mycobycterium tuberculosis
physiological function
-
like the raffinose ATP-binding protein RafK, the presence of the enzyme also activates the expression of raf operon genes. Enzyme-negative pneumococci show a significantly decreased expression of aga and rafEFG, but dihydrolipoamide dehydrogenase does not regulate rafK or the putative regulatory genes rafR and rafS. Dihydrolipoamide dehydrogenase also binds directly to RafK both in vitro and in vivo, indicating the possibility that dihydrolipoamide dehydrogenase regulates raffinose transport by a direct interaction with the regulatory domain of the transporter
physiological function
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
physiological function
-
RNA interference or the deletion of both alleles of lipoamide dehydrogenase in bloodstream Trypanosoma brucei results in an absolute requirement for exogenous thymidine. In the absence of thymidine, lipdh-/- parasites show a severely altered morphology and cell cycle distribution. Lipdh-/- cells are unable to infect mice. Degradation of branched-chain amino acids takes place but is dispensable. In cultured bloodstream - but not procyclic - African trypanosomes, the total cellular concentration of lipoamide dehydrogenase increases with increasing cell densities. In procyclic parasites, lipoamide dehydrogenasemRNA depletion causes an even stronger proliferation defect that is not reversed by presence of thymidine
physiological function
-
dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
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physiological function
-
LPD is a useful biocatalyst for regenerating NAD+
-
physiological function
-
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
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physiological function
Starkeyomyces koorchalomoides FDUS 0337
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
-
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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-(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+
-
-
-
-
?
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
-
-
?
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 + NADH
? + 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-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
-
-
?
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
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
-
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
-
-
?
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
-
-
?
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+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
233.4% activity compared to lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
233.4% activity compared to lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
12.3% of the activity with lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + 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
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 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
?
-
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
?
-
-
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
?
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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+
Q0KBV8
-
-
-
?
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
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
?
-
Q8NTE1
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
?
-
Q811C4
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
-
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
-
wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD
FAD
-
tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
-
the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates
FAD
-
a flavoprotein, each monomer of 51000 Da binds one molecule of FAD
NAD+
-
-
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
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+
-
-
393971, 393993, 394003, 394004, 659101, 672869, 673943, 674382, 674759, 674943, 675350, 677161, 691569, 711099
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 disulfide, the cofactor cycles between reduced and oxidized state during catalysis
-
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
-
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
-
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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.
INHIBITORS
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+
-
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
Diethylamine NONOate
-
induces 71% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
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)
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
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)
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-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
-
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
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
NADH
strong substrate inhibition at concentrations higher than 0.015 mM
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
p-Aminophenyldichloroarsine
-
inactivated only in presence of NADH and dihydrolipoamide, no significant loss of activity in absence of NADH and dihydrolipoamide
Zn2+
about 30% inhibition of recombinant BfmBC activity with 5 mM
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
-
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
-
no inhibition of the nitric oxide reduction by cyanide, antimycin A, or diphenyleneiodonium ions
-
additional information
-
LAD is not inhibited by resorufin ethyl ether, phenidone, Nomega-nitro-L-arginine methyl ester hydrochloride, proadiphen hydrochloride, and miconazole nitrate
-
additional information
-
no inhibition by the cation radical of 2-cyano-10-[3-(4-hydroxypiperidinyl)propyl]-dibenzothiazine in either peroxidase system
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
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
EDTA
-
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
lipoic acid
-
increase in activity might be due to formation of dihydrolipoic acid in the assay system
NAD+
0.2 mM NAD+ demonstrates a strong activating effect on LPD, and the activity is 5.2 times higher than that without NAD+
ubiquinone
-
slight increase in activity might be due to formation of ubiquinol in the assay system
additional information
-
activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation. Freezing-thawing results in further activation
-
additional information
-
activity of DLDH diaphorase is both protein amount- and time-dependent
-
additional information
-
activity of DLDH dehydrogenase increases in rats between 10 and 20 days of age. Dehydrogenase activity of DLDH shows a further, progressive increase in rats from 20 days to adulthood, in the absence of any further change in DLDH expression or diaphorase activity
-
additional information
-
activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation, Freezing–thawing results in further activation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.63
alpha-lipoamide
Starkeyomyces koorchalomoides
-
in 0.1 mM Tris-HCl (pH 7.0), 0.0005 mM EDTA, 0.01 mM beta2-mercaptoethanol, at 37°C
0.46
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.45
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.0157
Dihydrolipoamide
-
pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI
0.0177
Dihydrolipoamide
-
pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI
0.0243
Dihydrolipoamide
-
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.0274
Dihydrolipoamide
-
pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI
0.0364
Dihydrolipoamide
-
pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI
0.04
Dihydrolipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain
0.064
Dihydrolipoamide
-
recombinant DLDH expressed without lipoic acid