1.8.1.4: dihydrolipoyl dehydrogenase
This is an abbreviated version!
For detailed information about dihydrolipoyl dehydrogenase, go to the full flat file.
Word Map on EC 1.8.1.4
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1.8.1.4
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multienzyme
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fad
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acetyltransferase
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dehydrogenases
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alpha-ketoglutarate
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flavin
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branched-chain
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flavoproteins
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transacetylase
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thioredoxin
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azotobacter
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vinelandii
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thiamin
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subcomplexes
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alpha-keto
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acidosis
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alpha-ketoacids
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succinyltransferase
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mercuric
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flavoenzymes
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2-oxoacids
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trypanothione
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friedreich
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1.2.4.1
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subunit-binding
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two-electron
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radiofrequency
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medicine
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ketoacids
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degradation
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ashkenazi
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t-proteins
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myenteric
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analysis
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drug development
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diagnostics
- 1.8.1.4
-
multienzyme
- fad
- acetyltransferase
- dehydrogenases
- alpha-ketoglutarate
- flavin
-
branched-chain
- flavoproteins
- transacetylase
- thioredoxin
-
azotobacter
- vinelandii
- thiamin
-
subcomplexes
-
alpha-keto
- acidosis
- alpha-ketoacids
- succinyltransferase
-
mercuric
-
flavoenzymes
- 2-oxoacids
- trypanothione
- friedreich
-
1.2.4.1
-
subunit-binding
-
two-electron
-
radiofrequency
- medicine
-
ketoacids
- degradation
-
ashkenazi
-
t-proteins
-
myenteric
- analysis
- drug development
- diagnostics
Reaction
Synonyms
apicoplast E3, CDS, CIP50, coronin-interacting protein, dehydrogenase, lipoamide, dehydrolipoate dehydrogenase, DHLDH, DHLipDH, diaphorase, dihydrolipoamide dehydrogenase, dihydrolipoamide dehydrogenase E3, dihydrolipoamide:NAD+ oxidoreductase, dihydrolipoic dehydrogenase, dihydrolipomide dehydrogenase, dihydrolipoyl dehydrogenase, DLD, DLD1, Dld2, DLDH, DLDH dehydrogenase, DLDH diaphorase, DLDH2, DT-diaphorase, E3, E3 component, E3 component of 2-oxoglutarate dehydrogenase complex, E3 component of acetoin cleaving system, E3 component of alpha keto acid dehydrogenase complexes, E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes, E3 component of pyruvate complex, E3 lipoamide dehydrogenase, E3 protein component of 2-oxoacid dehydrogenase multienzyme complexes, E3 subunit of the alpha-ketoglutarate dehydrogenase complex, EC 1.6.4.3, Glycine cleavage system L protein, Glycine oxidation system L-factor, hDLDH, hE3, hLADH, L-protein, LAD, LADH, LDH, LDP-Glc, LDP-Val, LipDH, lipoamide dehydrogenase, lipoamide dehydrogenase (NADH), lipoamide dehydrogenase C, lipoamide dehydrogenase2, lipoamide oxidoreductase (NADH), lipoamide reductase, lipoamide-dehydrogenase-valine, lipoate dehydrogenase, lipoic acid dehydrogenase, lipoyl dehydrogenase, LPD, LPD-GLC, LPD-VAL, LPD1, LPD2, Lpd3, LpdA, LpdC, LpdG, LpdV, More, mtLPD2, NAD(P)H:lipoamide oxidoreductase, NADH dehydrogenase, NADH diaphorase, NADH:lipoamide oxidoreductase, nicotinamide adenine dinucleotide diaphorase, ORF-E3, pdhD, pdhL, PfaE3, rhDLDH, TAase, ubiquinone reductase
ECTree
1.8.1.4 dihydrolipoyl dehydrogenaseAdvanced search results
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results (KM Value
KM Value on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
3.63
alpha-lipoamide
Starkeyomyces koorchalomoides
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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
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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
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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
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recombinant DLDH expressed without without a lipoyl protein domain
0.064
dihydrolipoamide
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recombinant DLDH expressed without lipoic acid
0.64
dihydrolipoamide
wild type enzyme, at pH 8.0 and 37°C
15.83
formaldoxime
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
17.18
formaldoxime
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.27
glycerol trinitrate
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
16.93
glycerol trinitrate
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.56
Lipoamide
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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
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reaction with nicotinamide hypoxanthine dinucleotide
0.182
NAD+
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.186
NAD+
pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI
0.288
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+
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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
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.44
S-nitrosoglutathione
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.26
sodium nitroprusside
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in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
additional information
additional information
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dehydrogenase and oxidase activity kinetics
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additional information
additional information
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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
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additional information
additional information
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transient-state kinetics of reductive and oxidative half-reactions
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additional information
additional information
kinetic analysis and mechanisms of wild-type and mutant enzymes, overview
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additional information
additional information
kinetic analysis and modelling, detailed overview
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additional information
additional information
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kinetic analysis and modelling, detailed overview
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additional information
additional information
kinetic analysis and modelling, detailed overview
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additional information
additional information
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kinetic analysis and modelling, detailed overview
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additional information
additional information
kinetic analysis and modelling, detailed overview
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additional information
additional information
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kinetic analysis and modelling, detailed overview
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additional information
additional information
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Michaelis?Menten kinetics
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additional information
additional information
Michaelis?Menten kinetics
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