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Enzyme Nomenclature
Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
Word Map on EC 1.8.1.4
- 1.8.1.4
- fad
-
multienzyme
- alpha-ketoglutarate
- flavin
- disulfide
-
branched-chain
- flavoproteins
-
transacetylase
- vinelandii
-
azotobacter
-
subcomplexes
- thiamin
-
alpha-ketoacids
- acidosis
-
mercuric
-
alpha-keto
-
flavoenzymes
- trypanothione
-
succinyltransferase
- 2-oxoacids
- friedreich
-
two-electron
-
subunit-binding
-
t-proteins
- degradation
-
1.2.4.1
-
ashkenazi
- protochlorophyllide
-
frontotemporal
- medicine
- analysis
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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
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diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex; K-12
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dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex
-
-
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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
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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
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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
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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
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LPD is a useful biocatalyst for regenerating NAD+
-
physiological function
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enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
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physiological function
Starkeyomyces koorchalomoides FDUS 0337
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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
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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-methoxy phenazine methosulfate + NADH
? + NAD+
248.1% activity compared to lipoamide
-
-
?
1-methoxy phenazine 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+
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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
15.83
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
17.18
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.27
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
16.93
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.56
Lipoamide
-
reaction with 3-acetylpyridine adenine dinucleotide
3.3
Lipoamide
in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
6.4
Lipoamide
-
reaction with nicotinamide hypoxanthine dinucleotide
0.182
NAD+
-
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.19
NAD+
-
mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA; wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA
0.288
NAD+
-
pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI
0.292
NAD+
-
pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI
0.312
NAD+
-
pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI
0.82
NAD+
-
recombinant DLDH expressed without without a lipoyl protein domain
0.0061
NADH
in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
5.48
S-nitroso-N-acetylpenicillamine
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.44
S-nitrosoglutathione
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.26
sodium nitroprusside
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
additional information
additional information
-
transient-state kinetics of reductive and oxidative half-reactions
-
additional information
additional information
-
transient-state and steady-state kinetics of the enzyme in two-electron-reduced and four-electron-reduced state at 4°C and 25°C, respectively
-
additional information
additional information
-
dehydrogenase and oxidase activity kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
448
Dihydrolipoamide
Plasmodium falciparum
-
pH 8.0, 25°C, mitochondrial isozyme, reverse reaction, varying conditions
135.5 - 337
Lipoamide
Plasmodium falciparum
-
pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions
135.5 - 337
NAD+
Plasmodium falciparum
-
pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions
506
NAD+
Streptococcus pneumoniae
-
recombinant DLDH expressed without without a lipoyl protein domain
448
NADH
Plasmodium falciparum
-
pH 8.0, 25°C, mitochondrial isozyme, reverse reaction, varying conditions
additional information
additional information
Pisum sativum
-
turnover numbers for small polypeptides derived from proteolytic treatment of the H-protein
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000865
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
pH and temperature not specified in the publication
additional information
additional information
-
Zn2+ inhibition kinetics and mechanism
-
0.29
diphenyleneiodonium chloride
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.31
diphenyleneiodonium chloride
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.35
diphenyleneiodonium chloride
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.45
diphenyleneiodonium chloride
-
using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.56
diphenyleneiodonium chloride
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.6
diphenyleneiodonium chloride
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.8
diphenyleneiodonium chloride
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.0488
Lipoamide
-
recombinant DLDH expressed without lipoic acid, in the presence of 4 mM NAD+
0.1899
Lipoamide
-
recombinant DLDH expressed without lipoic acid, in the presence of 1.5 mM dihydrolipoamide
0.1953
Lipoamide
-
recombinant DLDH, in the presence of 1.5 mM dihydrolipoamide
0.349
Lipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 4 mM NAD+
0.8793
Lipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide
0.0044
NADH
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide
0.0107
NADH
-
recombinant DLDH expressed without lipoic acid, in the presence of 1.5 mM dihydrolipoamide
0.0149
NADH
-
recombinant DLDH, in the presence of 1.5 mM dihydrolipoamide
0.0351
NADH
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 2 mM NAD+
0.084
NADH
-
recombinant DLDH expressed without lipoic acid, in the presence of 2 mM NAD+
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]-N-[3-(trifluoromethyl)benzyl]acetamide
Mycobacterium tuberculosis
P9WHH8
pH and temperature not specified in the publication
0.0009
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
Mycobacterium tuberculosis
P9WHH8
pH and temperature not specified in the publication
0.59
diphenyleneiodonium chloride
Sus scrofa
-
using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.68
diphenyleneiodonium chloride
Sus scrofa
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.75
diphenyleneiodonium chloride
Sus scrofa
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.81
diphenyleneiodonium chloride
Sus scrofa
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.93
diphenyleneiodonium chloride
Sus scrofa
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.61
diphenyleneiodonium chloride
Sus scrofa
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
3.31
diphenyleneiodonium chloride
Sus scrofa
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.19
-
substrate 5,5'-dithiobis-(2-nitrobenzoic acid), 30°C, pH 6.5
2.5
crude extract, in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
6.4
6.65
19.3fold purified enzyme, in 50 mM potassium phosphate buffer, pH 6.7, at 37°C
16.2
-
pH 7.0, 30°C, mutant enzyme E423D, assay in the presence of 2 M KCI
20
59.2
after 23.9fold purification, in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
additional information
additional information
-
mutant P453V shows a specific activity of 0.37 units/mg at the saturated substrate concentrations of 2 mM dihydrolipoamide and 3 mM NAD+ at 37°C in a 50 mM potassium phosphate buffer (pH 8.0) containing 1.5 mM EDTA
additional information
-
wild type enzyme: 586.50 units/mg protein, mutant N286D: 179.65 units/mg protein, mutant N286Q: 143.15 units/mg protein, mutant D320N: 283.10 units/mg protein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
reduction of nitric oxide, lioamide, lipoic acid, and 2,6-dichlorophenolindophenol
7.4
7.5
8.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH 5.0: about 10% of maximal activity, pH 7.0-7.5: 60-70% of maximal activity, pH 8.0-8.5: 90% of maximal activity, pH 10.0: 10% of maximal activity in carbonate buffer
5.5 - 7.5
-
pH 5.5: about 75% of maximal activity, pH 7.5: about 40% of maximal activity, NADH-lipoamide oxidoreductase activity
6.5 - 8.5
-
pH 6.5: about 40% of maximal activity, pH 8.5: about 50% of maximal activity
7.5 - 8.8
-
pH 7.5: about 50% of maximal activity, pH 8.8: about 60% of maximal activity, dihydrolipoamide-NAD+ oxidoreductase activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme is not detected on Western blots probed with antibodies that recognize mitochondrial dihydrolipoamide dehydrogenase
additional information
-
both genes are transcribed during erythrocytic development of the parasite
-
30% increase in DLDH expression in rats between 10 and 20 days of age, whereas there is no further increase during the period from 20 to 60 days. Diaphorase activity shows a 46% increase in rats between 10 and 20 days of age, but there is also no further increase between 20 and 60 days. DLDH dehydrogenase activity increases progressively over the period from 10 to 60 days of age (63% between 10 and 20 days, 30% between 20 and 30 days, and 25% between 30 and 60 days of age)
-
significant increase in DLDH dehydrogenase activity in rats only for the period between 30 and 60 days of age
-
-
-
significant increase in DLDH dehydrogenase activity in rats only for the period between 30 and 60 days of age
-
increase in DLDH dehydrogenase activity in rats between 10 and 20 days of age, with no further increase evident thereafter
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to the matrix, release of enzyme during acrosomal exocytosis
-
-
juxtanuclear localization, like Golgi, in spermatids
additional information
-
Lpd1 protein is localized in the mitochondria during the logarithmic yeast growth and the filamentous growth
-
Lpd1 protein is localized in the mitochondria during the logarithmic yeast growth and the filamentous growth
-
-
isozyme mLipDH is a component of the branched-chain 2-ketoacid dehydrogenase and the 2-ketoglutarate dehydrogenase multienzyme complexes
-
enzyme is part of multienzyme complexes in the inner mitochondrial membrane
additional information
-
release of enzyme during acrosomal exocytosis, extramitochondrial localization in epididymal spermatozoa in mammalia
-
additional information
-
subcellular localization study using recombinant expression of the isozymes fused to fluorescent protein tags
-
additional information
-
synthesized predominantly on free ribosomes and translocated into mitochondria
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neisseria meningitidis serogroup B (strain MC58)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain UCBPP-PA14)
Pseudomonas aeruginosa (strain UCBPP-PA14)
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
-
recombinant protein using SDS-PAGE, in good agreement with the calculated molecular weight of recombinant DiaA
50000
50027
x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis
52000
53000
54000
55000
56000
57200
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
58000
75600
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
102000
105000
110000
112000
115000
119000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
-
x * 49757, mitochondrial enzyme, electrospray mass spectrometry; x * 52000, enzyme from chloroplast, SDS-PAGE; x * 52614, enzyme from chloroplast, electrospray mass spectrometry; x * 56000, mitochondrial enzyme, SDS-PAGE
?
-
x * 56000, enzyme from liver enzyme; x * 56000, SDS-PAGE; x * 58000, enzyme from heart, SDS-PAGE
dimer
x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis
dimer
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
homodimer
2 * 49912, calculated from amino acid sequence; 2 * 50000, SDS-PAGE
homodimer
-
2 * 49912, calculated from amino acid sequence; 2 * 50000, SDS-PAGE
-
additional information
-
the homodimeric enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
additional information
the enzyme is the E3 component of 2-keto acid dehydrogenase multienzyme complex
additional information
-
the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions
additional information
-
EC 1.8.1.4 is the E3-protein component of the mitochondrial 2-oxoacid dehydrogenase multienzyme complexes and the L-protein component of the glycine decarboxylase system
additional information
-
2 distinct dihydrolipoamide dehydrogenases, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
additional information
-
dihydrolipoamide dehydrogenase E3 is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, wheras it is bound to the pyruvate dehydrogenase complex through a protein X
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
-
the apicoplast isozyme contains a potential transit peptide, the mitochondrial isozyme contains targeting sequence
phosphoprotein
-
tyrosine-phosphorylated differently concerning time course in the principal piece of the flagella and the acrosome in capacitated spermatozoa, tyrosine-phosphorylation has regulatory function
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are grown from droplets of 0.002 ml of protein solution at 15 mg/ml and 0.002 ml of reservoir solution containing 10-20% polyethylene glycol 6000, 200 mM diammonium citrate, and 1 mM sodium azide
-
alone or in complex with inhibitor N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamide, hanging drop vapor diffusion method, using 100 mM Tris (pH 8.5), 10 mM NaCl, 11% (w/v) polyethylene glycol 10000, and 15% (v/v) ethylene glycol
best results obtained by vapour diffusion method, three-dimensional structure at 2.8 A resolution
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
enzyme loses its activity completely below pH 6 and above pH 11
702739
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
recombinant enzyme is stable at 30°C upon 30 min of incubation without substrates, but incubation at 40°C and higher temperatures inactivated enzyme activity
55 - 70
the remaining activity after thermal treatment at pH 7.0 for 15 min is 90% at 55°C, 80% at 60°C, 70% at 65 °C, and 45% at 70°C
65
70
75
-
50% loss of activity after 15 min, 50% loss of activity after 20 min in presence of NAD+, 50% loss of activity after less than 1 min in presence of dihydrolipoamide
95
100
additional information
65
-
the enzyme unfolds irreversibly at heat treatment higher than 65°C
95
-
15 min, in presence of 4 M NaCl, enzyme in crude extract, stable
95
-
15 min, in presence of 4 M NaCl, enzyme in crude extract, stable
additional information
-
in thepresence of 2 M KCI, the thermal stability properties of mutant enzymes E423S, E423Q and E423A are comparable to those of wild-type, although the mutants appear to be slightly more stable. Mutant enzyme E423D however, is inactivated at temperatures around 20°C lower than for the wild-type. In the absence of salt, similar relative thermostabilities are observed, but both wild-type and mutant enzymes are inactivated at temperatures around 16-18°C lower than in the presence of salt
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity when the enzyme is frozen at -20°C, and thawed three times
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, -20°C, 100 mM potassium phosphate, 100 mM KCl, pH 7.0, 1 mM EDTA, 50% v/v glycerol, stable for at least 1 year
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on propyllipoamide-glass columns
ammonium sulfate precipitation and Ni-NTA agarose column chromatography
Starkeyomyces koorchalomoides
-
by gel filtration
DEAE-Toyopearl 650 M column chromatography, butyl-Toyopearl 650 M column chromatography, and TSK-gel G3000SW gel filtration
dissociation of the lipoamide dehydrogenase component from the branched-chain alpha-keto acid dehydrogenase complex during purification
-
enzmye from culture supernatant of Clostridium kluyveri is purified using a DEAE-toyopearl column and a TSK-GEL G-3000 column. Recombinant protein is purified using a HiTrap chelating HP column
-
from pyruvate dehydrogenase complex
gel filtration
metal-affinity chromatography and Superdex 200 gel filtration chromatography
Ni-NTA-agarose resin column chromatography and Superdex 200 gel filtration
presence of dithiothreitol during purification preserves enzymatic activity
-
purified using copper-based metal ion affinity chromatography in the presence of 2 M KCl
-
recombinant His-tagged truncated isozymes from Escherichia coli by nickel affinity chromatography to 98% homogeneity
-
wild-type DLD and mutants purified by nickel affinity chromatography. C-term DLD purified to near homogeneity by a five-step procedure
-
from pyruvate dehydrogenase complex
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bfmBC gene encoding DLD. Ligated into vector pCR2.1, and introduced into Escherichia coli DH5alpha. Insert DNA recovered from the recombinant plasmid ligated into vector pET-28a(+), yielding pET-bfmBC and expressed in Escherichia coli BL21 (DE3)
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex, expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis of both lipdh genes using RT-PCR, expression of the mitochondrial isozyme as GFP-fusion protein giving green fluorescence and of the apicoplast isozyme fused to acyl-carrier-protein resulting in red fluorescence, expression of truncated mitochondrial and apicoplastic isozymes lacking the putative target sequences as His-tagged proteins in Escherichia coli strain BL21-RIL(DE3), the apicoplast isozyme is expressed at very low levels
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) Codon Plus RLI cells
expressed in Escherichia coli using the cytoplasmic expression vectors, pET3a and pET3d. Expressed as inclusion bodies and refolded by solubilisation in 8 M urea followed by dilution into a buffer containing 2 M KCl, 0.010 mM FAD, 1 mM NAD+, and 0.3 mM GSSG/3 mM GSH
-
expressed in Escherichia coli; His-tagged wild-type and mutant proteins overexpressed in Escherichia coli
-
expression in a strain of Haloferax volcanii lacking dihydrolipoamide dehydrogenase activity
-
expression in Escherichia coli
expression in Escherichia coli or in Corynebacterium glutamicum, the cloned gene is expressed in Corynebacterium glutamicum cells harbouring the gene on a plasmid shows 12fold higher specific LPD activity when compared to the wild-type strain
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
overexpressed in the parent organism by using the halophilic archaeal rRNA promoter
-
wild-type and mutant enzymes K37E, H452Q and E457Q; wild-type and mutant enzymes K37E, H452Q and E457Q, overexpression in Escherichia coli
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wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q, overexpression in Escherichia coli
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wild-type DLD and mutant D444V expressed in Escherichia coli BL21 with an N-terminal six-histidine tag. C-term DLD, the interface domain residing the proteolytic activity of DLD, expressed in Escherichia coli without any tags
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ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
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ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C44S
-
0.003% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature
C49S
-
0.012% of the activity of wild-type enzyme with NAD+ and dihydrolipoamide. Enzyme is capable to catalyze reactions with NADH as electron donor and ferricyanide, thio-NAD+, 2,6-dichlorophenol indophenol and O2 as electron acceptor. The fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature
K53R
-
spectral and redox properties of FAD in the mutant enzyme as well as the interaction of the flavin with bound NAD+ are profoundly affected by the mutation, K53R does not catalyze either the dihydrolipoamide-NAD+ or the NADH-lipoamide reactions except at very low concentrations of reducing substrate. The absorbance spectrum in the visible and near-ultraviolet is little changed from that of wild-type enzyme, in contrast to wild-type enzyme the spectrum of K53R is sensitive to pH. Unlike the wild-type enzyme, the binding of beta-NAD+ to K53R alters the spectrum
E354K
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is significantly less sensitive to NADH inhibition than the native LPD
H322Y
-
upon purification LPD loses activity and associated FAD at the gel filtration step
E423A
-
in 2 M KCl, the mutant is significantly less active than wild-type, decreased Km value for dihydrolipoamide. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423D
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wild-type and E423D mutant enzyme are much less active in the absence of KCl than in its presence. The mutant enzyme is inactivated at temperatures around 20°C lower than the wild-type
E423Q
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423S
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423A
-
in 2 M KCl, the mutant is significantly less active than wild-type, decreased Km value for dihydrolipoamide. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
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E423D
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wild-type and E423D mutant enzyme are much less active in the absence of KCl than in its presence. The mutant enzyme is inactivated at temperatures around 20°C lower than the wild-type
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E423Q
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
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E423S
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
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C45S
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Ser-45 mutant is highly purified, shows 5270fold lower activity than wild-type enzyme. Destroyed disulfide bond between Cys-45 and Cys-50 of the active disulfide center in human E3. UV-visible spectrum of the Ser-45 mutant is similar to that of the reduced form of the enzyme and the second fluorescence emission of the mutant disappears
C45Y
-
purification of the Tyr-45 mutant is not successful. Recombinant human E3 becomes too unstable to be easily obtained from Escherichia coli
D320N
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48.60% specific activity of the wild type enzyme, 82.7% of FAD content compared to that of the wild-type enzyme; specific activity is 48.6% to that of the wild-type E3. About 82.7% of FAD content compared to that of wild-type E3. Forms the dimer
D413A
-
the mutant shows 85% activity in the forward reaction and 79% activity in the reverse reaction compared to the wild type enzyme
D413N
-
the mutant shows 119% activity in the forward reaction and 96% activity in the reverse reaction compared to the wild type enzyme
D444V
D473L
-
site-directed mutagenesis, mutant shows about 37fold decreased activity and small conformational changes compared to the wild-type enzyme
E192Q
-
specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced
E340K
E431A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
E457Q
-
molar ratio of FAD to enzyme is 0.9 compared to 1 for the wild-type enzyme, mutation affects the environment surrounding FAD, decrease in efficiency of electron transfer from the reduced flavin to the oxidized substrate
H348A
-
the mutant shows 60% activity in the forward reaction and 66% activity in the reverse reaction compared to the wild type enzyme
H348L
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the mutant shows 65% activity in the forward reaction and 74% activity in the reverse reaction compared to the wild type enzyme
H450A
-
shows an increase in proteolytic activity as compared with the wild-type
H452Q
-
molar ratio of FAD to enzyme is 0.94 compared to 1 for the wild-type enzyme, no production of NADH when the enzyme is reduced by dihydrolipoamide, transfer of electrons from the substrate dihydrolipoamide to NAD+ is extremely low
I51A
-
mutant with about 100fold reduced activity compared to the wild type enzyme
K37E
K54E
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about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-value for lipoamide is increased by about twofold
N286D
-
30.84% specific activity of the wild type enzyme, 96% of FAD content compared to that of the wild-type enzyme; specific activity is 30.84% to that of the wild-type E3. About 96.0% of FAD content compared to that of wild-type E3. Forms the dimer
N286Q
-
24.57% specific activity of the wild type enzyme, 99.4% of FAD content compared to that of the wild-type enzyme; specific activity is 24.57% to that of the wild-type E3. About 99.4% of FAD content compared to that of wild-type E3. Forms the dimer
P325A
-
mutation of highly conserved resdue in the central domain, about 150fold decrease in kcat value
R281K
-
specific activity is 11.93% to that of wild-type E3. FAD-content is about 93% that of wild-type E3. Kcat of forward reaction is decreased dramatically. Substitution has no effect in the self-dimerization
R281N
-
specific activity is 12.50% to that of wild-type E3. FAD-content is about 96% that of wild-type E3. Kcat of forward reaction is decreased dramatically. Substitution has no effect in the self-dimerization
R447A
-
the mutant shows 110% activity in the forward reaction and 122% activity in the reverse reaction compared to the wild type enzyme
R447G
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 28% of that of the wild type enzyme
R460G
S456A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
S53K/K54S
-
about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced. The catalytic rate constant, turnover number/Km, is significantly lower than wild-type
T148G
-
specific activity is 76.34% to that of wild-type E3. FAD-content is about 710% that of wild-type E3. Substitution has no effect in the self-dimerization
T148S
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specific activity is 88.62% to that of wild-type E3. FAD-content is about 92% that of wild-type E3. Substitution has no effect in the self-dimerization
T44V
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site-directed mutagenesis, mutation of Thr44 of the FAD-binding region to Val, corresponding to the prokaryotic sequence, results in 2.2fold reduced activity with a slightly different microenvironment at the FAD-binding site
W366A
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mutation of highly conserved residue. kinetic parameters similar to wild-type
Y438A
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the mutant shows 100% activity in the forward reaction and 91% activity in the reverse reaction compared to the wild type enzyme
Y438F
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the mutant shows 100% activity in the forward reaction and 112% activity in the reverse reaction compared to the wild type enzyme
Y438H
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the mutant shows 99% activity in the forward reaction and 92% activity in the reverse reaction compared to the wild type enzyme
A181V
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
A290R
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
F269R
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
G312A/L313G/L314P/Q315M
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
L314P
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
N209V
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
R147T
the mutant is more sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
R347S
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
A181V
-
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
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A290R
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the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
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F269R
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the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
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N209V
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the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
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R147T
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the mutant is more sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
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additional information
D444V
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missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 12% of that of the wild type enzyme
D444V
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shows weak proteolytic activity with mature frataxin substrate, but consistently cleaves mature frataxin to denoted frataxin products with faster kinetics than the wild-type
E340K
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missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 38% of that of the wild type enzyme
K37E
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molar ratio of FAD to enzyme is 0.76 compared to 1 for the wild-type enzyme
R460G
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missense mutation, the dissociation constant is three orders of magnitude higher than that of wild-type E3
additional information
-
insertion mutant Mg7 has an insertion site between amino acids 222 and 223, preventing the expression of over 50% of the carboxyl-terminal portion of the 467-amino-acid protein, the mutant is classified as a potential virulence mutant
additional information
-
deletion of the LPD1 gene prevents oxidative stress in npt1DELTA and bna6DELTA mutants
additional information
-
protein expressed without lipoic acid is indistinguishable from the wild-type protein. The protein without a lipoyl protein domain has a 2-3fold higher turnover number, a lower Ki for NADH, and a higher Ki for lipoamide compared with the other two enzymes
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inactivation of the enzyme by guanidine-HCl is reversible by its removal
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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development of a blue native-PAGE-based method for isolation of enzymatically active DLDH from animal tissues and visualization as well as quantification of its diaphorase activity using the NADH/nitroblue tetrazolium detection system
degradation
medicine
additional information
degradation
-
shows flavin reductase activity with moderate diaphorase activity
degradation
B1IQM4
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
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decreased activity of DLDH induced by valproic acid metabolites may, at least in part, account for the impaired rate of oxygen consumption and ATP synthesis in mitochondria if 2-oxoglutarate or glutamate are used as respiratory substrates, thus limiting the flux of these substrates through the citric acid cycle
degradation
-
conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme
degradation
-
T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3
degradation
-
S456 and E431 form a catalytic dyad in the DLD monomer, whereas H450, by forming a hydrogen bond with E431, may decrease the ability of E431 to polarize the hydroxyl group of S456
medicine
-
dihydrolipoyl dehydrogenase is an important source of reactive oxygen species leading to life span limitation
medicine
-
mutations of the enzyme cause the often-fatal human disease known as E3 deficiency
medicine
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direct involvement of LpdC in the prolonged retention of coronin-1 on the phagosome, thus promoting phagosome maturation arrest. Under the influence of IFNgamma, LRG-47 is recruited to the phagosome and mediates dislocation of coronin-1 leading ultimately to phagosome acidification and recruitment of lysosomal vacuoles and phagolyosome fusion
medicine
-
direct involvement of LpdC in the prolonged retention of coronin-1 on the phagosome, thus promoting phagosome maturation arrest. Under the influence of IFNgamma, LRG-47 is recruited to the phagosome and mediates dislocation of coronin-1 leading ultimately to phagosome acidification and recruitment of lysosomal vacuoles and phagolyosome fusion
medicine
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NADH diaphorase staining can establish tissue non-viability after radiofrequency ablation, but the timing of staining after treatment must be considered when interpreting results to avoid false positive tests. Tissue that is apparently viable by NADH diaphorase staining within 2.5 hours of radiofrequency ablation may in fact have been ablated
medicine
-
brain DLDH expression and activity undergo independent postnatal maturational increases. Senescence does not confer any detectable change in the activity of DLDH or its susceptibility to inactivation by mitochondrial oxidative stress
medicine
-
linkage and association analysis of diplotypes in the DLD gene with Alzheimer's from the National Institute of Mental Health-National Cell Repository for Alzheimer's disease and Italian data series, controlling for Gender and ApoE e4 status. Significant evidence of association of DLD with Alzheimer's disease. Combining the linkage and association study results for DLD together, leads to a p-value that is more significant than any of the individual p-value results for DLD. Only with sufficiently large sample sizes it is possible to rule out whether the DLD gene is in fact associated with Alzheimer’s disease
medicine
-
lipoamide dehydrogenase activity and metallothionein levels may be critical for dopaminergic neuronal survival in Parkinson's disease. 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine can affect the lipoamide dehydrogenase activity and metallothionein content to exert its neurotoxicity
medicine
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
medicine
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lipoamide dehydrogenase activity and metallothionein levels may be critical for dopaminergic neuronal survival in Parkinson's disease. 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine can affect the lipoamide dehydrogenase activity and metallothionein content to exert its neurotoxicity
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medicine
-
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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additional information
high stability of rBfmBC may make it useful for practical use
additional information
-
high stability of rBfmBC may make it useful for practical use
additional information
metabolic context(s) of DLDHs remains an open question
additional information
-
metabolic context(s) of DLDHs remains an open question
additional information
-
a mutation in LPD leads to a pyruvate dehydrogenase complex that is less sensitive to inhibition by NADH, allowing the enzyme to function in an anaerobic culture, which changes the fermentation profile of the mutant. Presence and functional activity of such an NADH-insensitive pyruvate dehydrogenase may have significant unexplored physiological and biotechnological applications
additional information
-
the lipoyl protein domain (but not lipoic acid alone) plays a regulatory role in the enzymatic characteristics of pneumococcal DLDH
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