Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.8.1.4
-
RECOMMENDED NAME
GeneOntology No.
dihydrolipoyl dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
ping-pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
ping pong mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
involvement of a reversibly reducible disulfide bond in catalytic mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
Asp473 is important for efficient catalytic function of the enzyme
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
show the reaction diagram
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+
show the reaction diagram
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+
show the reaction diagram
the mitochondrial isozyme shows ping pong kinetic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
oxidation
-
catalyzes reoxidation of reduced lipoate attached to H-protein, a lipoic acid-containing protein
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
-
reduction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(S)-3-methyl-2-oxopentanoate dehydrogenase (acylating)
-
-
2-oxoglutarate decarboxylation to succinyl-CoA
-
-
2-oxoglutarate dehydrogenase complex
-
-
2-oxoisovalerate decarboxylation to isobutanoyl-CoA
-
-
4-methyl-2-oxopentanoate dehydrogenase (acylating)
-
-
acetyl CoA biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Citrate cycle (TCA cycle)
-
-
citric acid cycle
-
-
glycine cleavage
-
-
glycine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
Glycolysis / Gluconeogenesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
oxidative decarboxylation of pyruvate
-
-
pyruvate decarboxylation to acetyl CoA
-
-
Pyruvate metabolism
-
-
Valine, leucine and isoleucine degradation
-
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenase, lipoamide
-
-
-
-
dehydrolipoate dehydrogenase
-
-
-
-
DHLDH
-
-
-
-
DHLipDH
Q04829
-
DHLipDH
Haloferax volcanii DSM 3757
Q04829
-
-
diaphorase
-
-
-
-
diaphorase
-
-
dihydrolipoamide dehydrogenase
A4V929
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
Q8MUB0
-
dihydrolipoamide dehydrogenase
B1IQM4
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
P11959
-
dihydrolipoamide dehydrogenase
P09622
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
Q811C4
-
dihydrolipoamide dehydrogenase
B6F1A8
-
dihydrolipoamide dehydrogenase
Microbacterium luteolum JCM 9174
B6F1A8
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
Starkeyomyces koorchalomoides
-
-
dihydrolipoamide dehydrogenase
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
Q8VPK7
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
Streptomyces peucetius 29050
-
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
-
-
dihydrolipoamide dehydrogenase
P50970
-
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide:NAD+ oxidoreductase
-
-
dihydrolipoic dehydrogenase
-
-
-
-
dihydrolipoyl dehydrogenase
-
-
-
-
DLDH
-
-
-
-
DLDH
Q8MUB0
-
DLDH
Streptomyces peucetius 29050
-
-
-
DLDH
-
-
DLDH dehydrogenase
-
-
DLDH diaphorase
-
-
DLDH2
Pseudomonas aeruginosa ATCC 15692
Q9I3D1
-
-
DT-diaphorase
-
-
E3
-
-
-
-
E3
-
pyruvate dehydrogenase complex is composed of multiple copies of three catalytic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3)
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
P09622
-
EC 1.6.4.3
-
-
formerly
-
Glycine cleavage system L protein
-
-
-
-
Glycine oxidation system L-factor
-
-
-
-
L-protein
-
-
LADH
P09622
-
LADH
Starkeyomyces koorchalomoides
-
LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity
LADH
Starkeyomyces koorchalomoides FDUS 0337
-
LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity
-
LADH
-
-
LADH
P09623
-
LDP-Glc
-
-
-
-
LDP-Val
-
-
-
-
LipDH
-
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
Mus musculus C57/Bl-6
-
-
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
P9WHH8
-
lipoamide dehydrogenase
P9WHH8
-
-
lipoamide dehydrogenase
-
-
lipoamide dehydrogenase
P09623
-
lipoamide dehydrogenase (NADH)
-
-
-
-
lipoamide oxidoreductase (NADH)
-
-
-
-
lipoamide reductase
-
-
-
-
lipoamide-dehydrogenase-valine
-
-
lipoamide-dehydrogenase-valine
-
is the specific E3 subunit for branched-chain keto acid dehydrogenase
lipoamide-dehydrogenase-valine
Pseudomonas putida PpG2
-
is the specific E3 subunit for branched-chain keto acid dehydrogenase
-
lipoate dehydrogenase
-
-
-
-
lipoic acid dehydrogenase
-
-
-
-
lipoyl dehydrogenase
-
-
-
-
lipoyl dehydrogenase
-
-
LPD
-
-
-
-
LPD
Microbacterium luteolum JCM 9174
B6F1A8
-
-
LPD
Pseudomonas aeruginosa ATCC 15692
Q9I3D1
-
-
LPD-GLC
-
-
-
-
LPD-VAL
-
-
-
-
LPD1
-
plastidial LPD1 encodes one of the two E3 isoforms found in the plastidial pyruvate dehydrogenase complex
LPD1
Candida albicans CAI4
-
-
-
NAD(P)H:lipoamide oxidoreductase
-
-
NADH diaphorase
-
-
NADH diaphorase
-
-
NADH:lipoamide oxidoreductase
-
-
-
-
NADH:lipoamide oxidoreductase
A4V929
-
nicotinamide adenine dinucleotide diaphorase
-
-
ORF-E3
-
-
-
-
pdhL
Q0KBV8
-
pdhL
Cupriavidus necator ATCC 17699
Q0KBV8
-
-
TAase
Starkeyomyces koorchalomoides
-
Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity
TAase
Starkeyomyces koorchalomoides FDUS 0337
-
Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity
-
ubiquinone reductase
-
-
additional information
-
enzyme is a member of the pyridine nucleotide-disulfide oxidoreductase family of enzymes, enzyme is the E3 component of three different 2-ketoacid dehydrogenase multienzyme complexes, i.e. the pyruvate, 2-ketoglutarate, and branched chain 2-keto acid dehydrogenase complexes
additional information
-
enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
additional information
-
the enzyme is the E3 component of the pyruvate dehydrogenase multienzyme complex
additional information
-
enzyme belongs to the family of pyridine nucleotide oxidoreductases
CAS REGISTRY NUMBER
COMMENTARY
9001-18-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotypes Col-0 and Col-2
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
Azotobacter agilis
-
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
Candida albicans CAI4
-
-
-
Manually annotated by BRENDA team
strain ATCC 8527
UniProt
Manually annotated by BRENDA team
Corynebacterium glutamicum DSM 20300
-
Uniprot
Manually annotated by BRENDA team
Cupriavidus necator ATCC 17699
-
UniProt
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3; K-12
-
-
Manually annotated by BRENDA team
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex
-
-
Manually annotated by BRENDA team
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex; K-12
-
-
Manually annotated by BRENDA team
K-12; strain B; strain Crookes; strain M191-6
-
-
Manually annotated by BRENDA team
Escherichia coli Crookes
strain Crookes
-
-
Manually annotated by BRENDA team
strains AH242 SE2378 and SE2382
-
-
Manually annotated by BRENDA team
Escherichia coli M191-6
strain M191-6
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
Haloferax volcanii DSM 3757
-
SwissProt
Manually annotated by BRENDA team
Microbacterium luteolum JCM 9174
-
UniProt
Manually annotated by BRENDA team
C57/Bl-6 mice
-
-
Manually annotated by BRENDA team
C57BL6 male mice
-
-
Manually annotated by BRENDA team
Mus musculus C57/Bl-6
C57/Bl-6 mice
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium smegmatis
-
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
3D7, 2 lipdh genes encoding 2 isozymes in mitochondrion and apicoplast, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa ATCC 15692
-
UniProt
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
strain PpG2
-
-
Manually annotated by BRENDA team
two lipoamide dehydrogenases: LPD-glc and LPD-val
-
-
Manually annotated by BRENDA team
Pseudomonas putida PpG2
strain PpG2
-
-
Manually annotated by BRENDA team
adult Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
female and male Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
Starkeyomyces koorchalomoides
-
-
-
Manually annotated by BRENDA team
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
Manually annotated by BRENDA team
Streptomyces peucetius 29050
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
dihydrolipoamide dehydrogenase E3
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
PCC6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
Candida albicans CAI4
-
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
-
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
-
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
-
last step of glycine cleavage system
physiological function
-
dihydrolipoamide dehydrogenase is a FAD-linked subunit of 2-oxooglutarate, pyruvate and branched-chain amino acid dehydrogenases and the glycine cleavage system, transfering electrons from the dihydrolipoic acid prosthetic group to the NAD+ cofactor via its FAD center
physiological function
-
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
B6F1A8
LPD is a useful biocatalyst for regenerating NAD+
physiological function
-
plastidial LPD expression quantitatively controls Arabidopsis arsenate sensitivity
physiological function
Starkeyomyces koorchalomoides
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
physiological function
Q9I3D1
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
-
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
-
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
-
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
Pseudomonas aeruginosa ATCC 15692
-
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
Microbacterium luteolum JCM 9174
-
LPD is a useful biocatalyst for regenerating NAD+
-
physiological function
Starkeyomyces koorchalomoides FDUS 0337
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
-
physiological function
Candida albicans CAI4
-
dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
show the reaction diagram
-
-
-
-
?
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
show the reaction diagram
-
-
-
-
?
1-methoxy phenazine methosulfate + NADH
? + NAD+
show the reaction diagram
Microbacterium luteolum, Microbacterium luteolum JCM 9174
B6F1A8
248.1% activity compared to lipoamide
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
show the reaction diagram
-
31.1% of the activity with lipoamide
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
show the reaction diagram
-
cytochrome c is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
Q8NTE1
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
A5N930
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
-
12.3% of the activity with lipoamide
-
-
?
2,6-dichlorophenolindophenol + NADH
? + NAD+
show the reaction diagram
Microbacterium luteolum, Microbacterium luteolum JCM 9174
B6F1A8
233.4% activity compared to lipoamide
-
-
?
2,6-dimethoxy-1,4-benzoquinone + NADH
? + NAD+
show the reaction diagram
B6F1A8
8.0% activity compared to lipoamide
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
show the reaction diagram
-
-
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
show the reaction diagram
-
90fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
-
-
?
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
show the reaction diagram
Q8NTE1
-
-
-
?
2-hydroxy-1,4-benzoquinone + NADH
2-hydroxy-1,4-benzoquinol + NAD+
show the reaction diagram
-
-
-
-
?
2-methyl-1,4-benzoquinone + NADH
2-methyl-1,4-benzoquinol + NAD+
show the reaction diagram
-
-
-
-
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + NAD(P)H
3-aminotyrosine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + NADPH
3-aminotyrosine + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
show the reaction diagram
Q0KBV8
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
show the reaction diagram
Cupriavidus necator ATCC 17699
Q0KBV8
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADH
5-hydroxy-1,4-naphthoquinol + NAD+
show the reaction diagram
-
-
-
-
?
5-nitroblue tetrazolium chloride + NADH
? + NAD+
show the reaction diagram
-
5.1% of the activity with lipoamide
-
-
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
show the reaction diagram
-
-
-
-
?
8-nitroguanine + NAD(P)H
8-aminoguanine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
8-nitroguanine + NADPH
8-aminoguanine + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + NAD(P)H
8-aminoxanthine + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + NADPH
8-aminoxanthine + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
acetaldoxime + NADH
?
show the reaction diagram
-
-
-
-
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
Starkeyomyces koorchalomoides, Starkeyomyces koorchalomoides FDUS 0337
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
Q0KBV8
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
Cupriavidus necator ATCC 17699
Q0KBV8
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
show the reaction diagram
-
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
show the reaction diagram
Q0KBV8
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
show the reaction diagram
-
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
show the reaction diagram
Cupriavidus necator ATCC 17699
Q0KBV8
-
-
-
?
benzyl viologen + NADH
? + NAD+
show the reaction diagram
-
2.9% of the activity with lipoamide
-
-
?
coenzyme Q-10 + NADPH
ubiquinol + NADP+
show the reaction diagram
Mus musculus, Mus musculus C57/Bl-6
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
-
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
-
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
O81413
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
-
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Q8NTE1
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Azotobacter agilis
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
A5N930
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Q8MUB0
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Q04829
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
P9WHH8
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
mutant enzymes C44S and C49S show minute activity
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
alternate oxidation and reduction of an intrachain disulfide bond
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
the forward reaction is the physiological one
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
A4V929
DLDH activity, forward reaction
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Synechocystis sp. PCC6803
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Pseudomonas putida PpG2
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
P9WHH8
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Candida albicans CAI4
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Haloferax volcanii DSM 3757
Q04829
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Haloferax volcanii DSM 3757
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
Escherichia coli Crookes, Escherichia coli M191-6
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
P09622
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
P09622
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
P9WHH9
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
P09623
-
-
-
?
dihydrolipoamide + NADP+
lipoamide + NADPH
show the reaction diagram
-
-
-
r
DL-6,8-thiooctic acid amide + NADH
? + NAD+
show the reaction diagram
-
-
-
-
r
DL-alpha-lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
show the reaction diagram
Streptomyces peucetius, Streptomyces peucetius 29050
-
specific substrate
-
-
?
DL-lipoate + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
DL-lipoylbutanoate + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
DL-lipoylpentanoate + NADH
? + NAD+
show the reaction diagram
-
100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state
-
-
?
ferrocene + NADH
? + NAD+
show the reaction diagram
B6F1A8
3.6% activity compared to lipoamide
-
-
?
ferrocenecarboxylic acid + NADH
? + NAD+
show the reaction diagram
B6F1A8
4.1% activity compared to lipoamide
-
-
?
formaldoxime + NADH
?
show the reaction diagram
-
-
-
-
?
glycerol trinitrate + NADH
?
show the reaction diagram
-
-
-
-
?
hexacyanoferrate + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
hydroxylamine hydrochloride + NADH
?
show the reaction diagram
-
-
-
-
?
iodonitrotetrazolium + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
iodonitrotetrazolium chloride + NADH
? + NAD+
show the reaction diagram
B6F1A8
19.3% activity compared to lipoamide
-
-
?
lipoamide + 3-acetylpyridine adenine dinucleotide
dihydrolipoamide + ?
show the reaction diagram
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
P09622
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
O81413
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
A5N930
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
Q8MUB0
-
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
B6F1A8
100% activity
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
A4V929
NADH:lipoamide oxidoreductase activity, reverse reaction
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
Microbacterium luteolum JCM 9174
B6F1A8
100% activity
-
-
?
lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
P09622
-
-
-
?
lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
r
lipoamide + nicotinamide hypoxanthine dinucleotide
dihydrolipoamide + ?
show the reaction diagram
-
-
-
-
?
lipoamide + thio-NADH
dihydrolipoamide + thio-NAD+
show the reaction diagram
-
-
-
-
?
lipoic acid + NADH
dihydrolipoic acid + NAD+
show the reaction diagram
-
-
-
-
?
lipoic acid + NADH
dihydrolipoic acid + NAD+
show the reaction diagram
-
-
-
-
?
lipoic acid + NADH
dihydrolipoic acid + NAD+
show the reaction diagram
-
-
-
-
r
mature frataxin + NADH
denoted frataxin + NAD+
show the reaction diagram
-
cleavage by C-term DLD
-
-
?
mature frataxin + NADH
denoted frataxin + NAD+
show the reaction diagram
-
exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity
-
-
?
menadione + NADH
? + NAD+
show the reaction diagram
-
13.6% of the activity with lipoamide
-
-
?
menadione + NADH
? + NAD+
show the reaction diagram
Microbacterium luteolum, Microbacterium luteolum JCM 9174
B6F1A8
2.9% activity compared to lipoamide
-
-
?
methylene blue + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
methylene blue + NADH
? + NAD+
show the reaction diagram
-
9.4% of the activity with lipoamide
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
show the reaction diagram
-
-
-
-
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
show the reaction diagram
-
-
-
-
?
nitrated DNA + NAD(P)H
?
show the reaction diagram
-
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
show the reaction diagram
-
enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination
-
-
?
nitric oxide + NADH
nitrate + NAD+
show the reaction diagram
-
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
nitro blue tetrazolium + NADH
? + NAD+
show the reaction diagram
A5N930
-
-
-
?
nitrotetrazolium blue + NADH
? + NAD+
show the reaction diagram
B6F1A8
2.9% activity compared to lipoamide
-
-
?
O2 + NADH
?
show the reaction diagram
-
-
-
-
?
O2 + NADH
?
show the reaction diagram
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
O2 + NADH
H2O2 + NAD+
show the reaction diagram
-
-
-
-
?
O2 + NADH
H2O2 + NAD+
show the reaction diagram
-
-
-
-
?
O2 + NADH
H2O2 + NAD+
show the reaction diagram
-
40fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
-
-
?
O2 + NADH
H2O2 + NAD+
show the reaction diagram
-
the enzyme produces reactive oxygen species, i.e. hydrogen peroxide, acting as an oxidase
-
-
?
O2 + NADH + H+
H2O2 + NAD+
show the reaction diagram
-
-
-
-
?
oxidized lipoamide + NADH
reduced lipoamide + NAD+
show the reaction diagram
-
-
-
-
?
oxidized lipoic acid + NADH
reduced lipoic acid + NAD+
show the reaction diagram
-
-
-
-
?
pyruvate + NADH
?
show the reaction diagram
-
-
-
-
?
reduced DL-lipoamide + NAD+
oxidized DL-lipoamide + NADH
show the reaction diagram
-
-
-
-
r
reduced lipoamide + NAD+
oxidized lipoamide + NADH
show the reaction diagram
-
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
resazurin + NADH
? + NAD+
show the reaction diagram
B6F1A8
155.8% activity compared to lipoamide
-
-
?
resorufin + NADH
? + NAD+
show the reaction diagram
B6F1A8
19.1% activity compared to lipoamide
-
-
?
S-nitroso-N-acetylpenicillamine + NADH
?
show the reaction diagram
-
-
-
-
?
S-nitrosoglutathione + NADH
?
show the reaction diagram
-
-
-
-
?
sodium nitroprusside + NADH
?
show the reaction diagram
-
-
-
-
?
sulfonated tetrazolium + NADH
? + NAD+
show the reaction diagram
B6F1A8
39.2% activity compared to lipoamide
-
-
?
tellurite + NADH
NAD+ + ?
show the reaction diagram
-
-
-
-
?
tellurite + NADH
NAD+ + ?
show the reaction diagram
P50970
-
-
-
?
tellurite + NADH
NAD+ + ?
show the reaction diagram
Q8VPK7
-
-
-
?
tellurite + NADH
NAD+ + ?
show the reaction diagram
P11959
-
-
-
?
tellurite + NADH
NAD+ + ?
show the reaction diagram
B1IQM4
-
-
-
?
thio-NAD+ + NADH
thio-NADH + NAD+
show the reaction diagram
-
-
-
-
?
thio-NAD+ + NADH
thio-NADH + NAD+
show the reaction diagram
-
-
-
-
?
thio-NAD+ + NADH
thio-NADH + NAD+
show the reaction diagram
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
-
-
-
-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
-
-
-
-
ir
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
-
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)+
show the reaction diagram
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
vitamin K5 + NADH
?
show the reaction diagram
-
-
-
-
?
metmyoglobin + NADH
reduced myoglobin + NAD+
show the reaction diagram
-
myoglobin is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
-
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
?
-
-
NADH:NAD+ transhydrogenase activity
-
-
-
additional information
?
-
-
reductive half-reaction, hydride transfer from NADH to FAD, is rate limiting when a quinone is the oxidant
-
-
-
additional information
?
-
-
diaphorase activity
-
-
-
additional information
?
-
-
diaphorase activity
-
-
-
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
-
-
-
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
?
-
-
lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
-
-
-
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 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
?
-
Q8NTE1
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
-
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 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
?
-
-
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 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
?
-
B6F1A8
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
-
additional information
?
-
-
enzyme lacks diaphorase activity
-
-
-
additional information
?
-
Microbacterium luteolum JCM 9174
B6F1A8
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
Q0KBV8
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
show the reaction diagram
Cupriavidus necator ATCC 17699
Q0KBV8
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
-
r
nitrated DNA + NAD(P)H
?
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes
-
-
r
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
-
-
-
-
ir
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
show the reaction diagram
-
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)+
show the reaction diagram
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
-
the forward reaction is the physiological one
-
-
r
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
-
-
-
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
?
-
-
lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
-
-
-
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 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
?
-
Q8NTE1
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
-
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 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
?
-
-
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 might play a role in modifying NO levels under specific cell conditions
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dihydrolipoic acid
-
-
FAD
-
2 molecules of FAD per molecule of enzyme
FAD
-
contains 1 FAD per subunit
FAD
-
contains 1 FAD per subunit
FAD
-
contains 1 FAD per subunit
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
-
contains one noncovalently bound FAD per subunit
FAD
-
contains 1 FAD per subunit
FAD
-
0.01882 mM of FAD per mg of protein
FAD
O81413
covalently bound to the protein
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
-
contains 1 FAD per subunit
FAD
-
contains 1 FAD per subunit
FAD
-
contains one noncovalently bound FAD per subunit
FAD
-
protein-bound
FAD
-
tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
-
flavoenzyme, 1 FAD per enzyme subunit, functionally important
FAD
Q811C4
binding site amino acid sequence
FAD
-
1 FAD as prosthetic group per enzyme subunit
FAD
-
prosthetic group, 1 FAD per enzyme subunit
FAD
-
the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates
FAD
-
the enzyme contains 1 functionally important FAD per subunit
FAD
A5N930
contains a noncovalently but tightly attached FAD molecule
FAD
-
contains one FAD as a prosthetic group in each subunit
FAD
Starkeyomyces koorchalomoides
-
-
FAD
-
-
FAD
B6F1A8
1.34 mol FAD per 1 mol of subunit of the enzyme
FAD
Q8MUB0
-
NAD(P)H
-
NADH is the preferred cofactor
NAD(P)H
-
NADPH and NADH are equally effective as cofactors
NAD(P)H
-
NADPH and NADH are utilized at similar rates for ubiquinone reduction
NAD+
-
highly specific for
NAD+
Azotobacter agilis
-
-
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+
O81413
-
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+
-
highly specific for
NAD+
-
dependent on
NAD+
A4V929
NAD+ is prefered
NAD+
Q8MUB0
-
NADH
-
highly specific for
NADH
-
-
NADH
O81413
-
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
NADH
-
highly specific for
NADH
A5N930
has a preference for NADH as a coenzyme
NADH
Starkeyomyces koorchalomoides
-
-
NADH
-
-
NADH
B6F1A8
high affinity for NADH, no activity with NADPH
NADH
-
highly specific
NADH
Q0KBV8
highly specific
NADP+
-
no activity
NADP+
A4V929
-
NADPH
-
no activity
NADPH
-
oxidizes NADPH as efficiently as NADH
NADPH
-
-
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
-
enzyme contains 1 disulfide/dithiol per subunit
-
additional information
-
no activity with NADH
-
additional information
-
no activity with NADPH
-
additional information
-
the enzyme contains 1 disulfide/dithiol per subunit
-
additional information
-
contains neither FMN nor FAD in the molecule
-
additional information
A5N930
FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
-
additional information
-
no activity with NADPH
-
additional information
-
unable to use NADP+ and NADPH
-
additional information
-
no cofactor: NADPH
-
additional information
Q0KBV8
no cofactor: NADPH
-
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
KCl
-
maximal enzymatic activity at 2 to 3 M KCl
NaCl
-
completely inactive in absence of NaCl
Zn2+
-
highly stimulating for ubiquinone reduction
Zn2+
-
highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM, Zn2+ slightly elevates the pH-optimum of the enzyme
Zn2+
-
highly activating ubiquinone reduction, up to 0.5 mM
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
additional information
A5N930
1 mM Na+, Ca2+, Mg2+, Mn2+, Fe3+, Zn2+, Pb2+, and Hg2+ do not enhance enzyme activity
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
P9WHH8
-
5-methoxyindole-2-carboxylic acid
Q811C4
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
Angeli's salt
-
at 2 mM, induces a 90% loss in DLDH diaphorase activity
arsenite
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
arsenite
-
0.3 mM, 50% inhibition
arsenite
-
reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity
Cd2+
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
chlorpromazine
-
0.1 mM, 75% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 94% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 89% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
Diethylamine NONOate
-
induces 71% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
Dihydrolipoamide
-
-
diisopropyl fluorophosphate
-
fully inhibits activity of the C-term protein
diisopropyl fluorophosphate
-
DLD is fully inactivated by 1 mM
diphenyleneiodonium chloride
-
-
Fe2+
-
at high concentrations has significant inhibitory effect on the lipoamide dehydrogenase activity
fluphenazine
-
0.1 mM, 53% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 61% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
folic acid
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
Guanidine-HCl
-
4C: 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+
A5N930
1 mM shows strong inhibitory effect on recombinant rBfmBC activity (more than 80% inhibition)
iodoacetic acid
-
in presence of NADH or dihydrolipoamide
isobiopterin
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
-
N-ethylmaleimide
-
over 90% inhibition at 1 mM
N-ethylmaleimide
-
induces more than 95% loss in DLDH diaphorase 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
P9WHH8
most potent inhibitor, noncompetitive versus NADH, NAD+, and lipoamide
NAD(P)+
-
product inhibition
NAD+
-
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
NAD+
-
product inhibition of the oxygen oxidase activity
NADH
-
competitive with respect to NAD+
NADH
-
competitive with respect to NAD+
NADH
-
chloroplastic enzyme is more susceptible to product inhibition than the mitochondrial enzyme
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
A4V929
strong substrate inhibition at concentrations higher than 0.015 mM
p-Aminophenyldichloroarsine
-
inactivated only in presence of NADH and dihydrolipoamide, no significant loss of activity in absence of NADH and dihydrolipoamide
p-Aminophenyldichloroarsine
-
in presence of NADH
p-Aminophenyldichloroarsine
-
-
p-[(bromoacetyl)-amino]phenyl arsenoxide
-
irreversible active site directed inactivation
Pb2+
A5N930
1 mM shows strong inhibitory effect on recombinant BfmBC activity (more than 80% inhibition)
PCMB
-
0.1 mM, 50% inhibition
perphenazine
-
0.1 mM, 69% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 75% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 79% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
phenothiazine cation radicals
-
irreversible inactivation dependent on time, radical structure, and radical production enzyme system, radicals are produced by reaction of myeloperoxidase or horse radish peroxidase on the phenothiazines promazine, trimeprazine, thioridazine, chlorpromazine, prochlorperazine, promethazine, and others, in presence of H2O2, protection by radical scavengers e.g. thiol compounds, amino acids and peptides, pyridine dinucleotides like NADH, or best by ascorbate and trolox, overview
potassium phosphate
-
when purified DLDH is eluted directly into potassium phosphate buffer, the enzymatic activity rapidly decreases
prochlorperazine
-
0.1 mM, 80% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 85% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 80% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
promazine
-
0.1 mM, 89% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 93% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 94% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4, 94% inhibition in the presence of 0.2 mM NADH, 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 after 10 min incubation
Promethazine
-
0.1 mM, 79% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 51% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 72% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
propericyazine
-
0.1 mM, 40% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4
propionylpromazine
-
0.1 mM, 32% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 88% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 83% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
S-nitrosocysteine
-
induces a 62% loss in diaphorase activity at 2 mM and an 88% loss at 10 mM
S-nitrosoglutathione
-
induces 84% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
thioridazine
-
0.1 mM, 82% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 97% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 85% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4, 85% inhibition in the presence of 0.1 mM NADH, 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 after 10 min incubation
Trifluoperazine
-
0.1 mM, 16% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 72% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 67% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
triflupromazine
-
0.1 mM, 68% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 16% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
trimeprazine
-
0.1 mM, 90% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 90% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 94% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
valproyl-CoA
-
competitive inhibitor, 0.5-1.0 mM inhibit DLDH activity
valproyl-dephosphoCoA
-
uncompetitive inhibitor, 0.5-1.0 mM inhibit DLDH activity
Zn2+
-
reversible binding, competitive to lipoamide, uncompetitive to NADH
Zn2+
A5N930
about 30% inhibition of recombinant BfmBC activity with 5 mM
additional information
-
no inhibition by iodoacetate
-
additional information
-
no inhibition of the nitric oxide reduction by cyanide, antimycin A, or diphenyleneiodonium ions
-
additional information
-
no inhibition by the cation radical of 2-cyano-10-[3-(4-hydroxypiperidinyl)propyl]-dibenzothiazine in either peroxidase system
-
additional information
-
inhibited by caloric restriction
-
additional information
-
diamide, GSH, GSSG, cysteine and nitrite do not exhibit any inhibitory effects
-
additional information
-
expression of LRG-47, as well as IFNgamma stimulation, block intracellular interaction of coronin-1 with LpdC
-
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
-
calcium and copper do not affect the enzyme activity
-
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
-
enzyme is sensitive to air-inactivation
-
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
dithiothreitol
-
presence during purification preserves enzymatic activity
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
Guanidine-HCl
-
4C: activates the enzyme 2.5fold at 0.2 M
KCl
-
4C: activates the enzyme at concentrations below 1 M
lipoic acid
-
increase in activity might be due to formation of dihydrolipoic acid in the assay system
NaCl
-
4C: activates the enzyme at concentrations below 1 M
NAD+
B6F1A8
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
Zn2+
-
stimulates the oxygen oxidase activity of the enzyme
Zn2+
-
dose dependently enhances the lipoamide dehydrogenase activity
methylene blue
-
stimulates reduction of cytochrome c and myoglobin
additional information
-
no activation by urea
-
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
-
additional information
-
activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation, Freezingthawing results in further activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
1,4-benzoquinone
-
-
0.4
1,4-benzoquinone
-
-
0.05
1,4-Naphthoquinone
-
-
0.015
2,6-dichlorophenolindophenol
-
-
0.03
2,6-dichlorophenolindophenol
-
-
0.12
2,6-dichlorophenolindophenol
A5N930
in diaphorase activity
0.86
2,6-dimethyl-1,4-benzoquinone
-
-
0.46
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
1.45
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.39
3-acetylpyridine adenine dinucleotide
-
-
0.29
5-hydroxy-1,4-naphthoquinone
-
-
0.96
acetaldoxime
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
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 37C
0.0107
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423A
0.0157
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423D, assay in the absence of KCI
0.017
Dihydrolipoamide
-
-
0.0177
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423Q, assay in the absence of KCI
0.018
Dihydrolipoamide
-
pH 8.0, 37C
0.0228
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423Q
0.023
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423S
0.0243
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423A, assay in the absence of KCI
0.025
Dihydrolipoamide
-
-
0.0266
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423D
0.0269
Dihydrolipoamide
-
pH 7.0, 30C, wild-type enzyme
0.0274
Dihydrolipoamide
-
pH 7.0, 30C, wild-type enzyme, assay in the absence of KCI
0.0364
Dihydrolipoamide
-
pH 7.0, 30C, mutant enzyme E423S, assay in the absence of KCI
0.04
Dihydrolipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain
0.046
Dihydrolipoamide
-
37C, pH 8.0
0.05
Dihydrolipoamide
-
mutant enzyme S53K/K54S
0.056
Dihydrolipoamide
-
recombinant DLDH
0.064
Dihydrolipoamide
-
recombinant DLDH expressed without lipoic acid
0.08
Dihydrolipoamide
-
complex-bound dihydrolipoamide dehydrogenase
0.09
Dihydrolipoamide
-
mutant P325A, pH 8.0, 37C, presence of 1.5 mM EDTA
0.12
Dihydrolipoamide
-
mutant enzyme E192Q
0.12
Dihydrolipoamide
-
mutant R281K
0.13
Dihydrolipoamide
-
-
0.146
Dihydrolipoamide
-
pH 8.0, 25C, mitochondrial isozyme
0.2
Dihydrolipoamide
-
mutant enzyme N286Q; mutant N286Q
0.28
Dihydrolipoamide
-
free dihydrolipoamide dehydrogenase
0.3
Dihydrolipoamide
A5N930
-
0.38
Dihydrolipoamide
-
wild-type; wild type enzyme
0.38
Dihydrolipoamide
-
mutant R281N; wild-type E3
0.4
Dihydrolipoamide
-
-
0.48
Dihydrolipoamide
-
-
0.58
Dihydrolipoamide
-
mutant T148G
0.58
Dihydrolipoamide
-
mutant W366A, pH 8.0, 37C, presence of 1.5 mM EDTA
0.59
Dihydrolipoamide
-
mutant T148S
0.64
Dihydrolipoamide
-
wild-type, pH 8.0, 37C, presence of 1.5 mM EDTA
0.69
Dihydrolipoamide
-
native enzyme
0.7
Dihydrolipoamide
-
mutant enzyme N286D; mutant N286D
0.7
Dihydrolipoamide
A4V929
-
0.76
Dihydrolipoamide
-
mutant enzyme K37E
0.83
Dihydrolipoamide
-
-
0.88
Dihydrolipoamide
-
wild-type enzyme
1.21
Dihydrolipoamide
-
mutant D320N; mutant enzyme D320N
2.9
Dihydrolipoamide
-
mutant enzyme H457Q
43.6
Dihydrolipoamide
-
mutant enzyme H452Q
4.7
dihydrolipoate
-
-
0.029
ferric leghemoglobin
O81413
-
-
2.73
formaldoxime
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
15.83
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
17.18
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
17.82
formaldoxime
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.9
glycerol trinitrate
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
1.42
glycerol trinitrate
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
2.27
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
16.93
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.027
H-protein
-
-
-
3.24
Hydroxylamine hydrochloride
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.05
Lipoamide
-
mutant enzyme N286Q; mutant N286Q
0.07
Lipoamide
-
mutant enzyme N286D; mutant N286D
0.31
Lipoamide
-
mutant enzyme E192Q
0.37
Lipoamide
-
-
0.42
Lipoamide
A5N930
-
0.46
Lipoamide
-
mutant D320N; mutant enzyme D320N
0.56
Lipoamide
-
reaction with 3-acetylpyridine adenine dinucleotide
0.56
Lipoamide
-
wild-type; wild type enzyme
0.63
Lipoamide
-
mutant enzyme S53K/K54S
0.87
Lipoamide
-
pH 8.0, 25C, mitochondrial isozyme
1.26
Lipoamide
A4V929
-
1.3
Lipoamide
-
-
2.25
Lipoamide
-
wild-type enzyme
3.3
Lipoamide
B6F1A8
in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25C
3.38
Lipoamide
O81413
-
3.7
Lipoamide
-
-
5
Lipoamide
-
-
5
Lipoamide
-
mutant enzyme K54E
5.8
Lipoamide
-
reaction with thio-NADH
6.4
Lipoamide
-
reaction with nicotinamide hypoxanthine dinucleotide
16
Lipoamide
-
reaction with NADH
2.1
lipoic acid
-
-
0.037
NAD+
-
-
0.045
NAD+
-
pH 8.0, 25C, mitochondrial isozyme
0.06
NAD+
-
mutant P325A, pH 8.0, 37C, presence of 1.5 mM EDTA
0.07
NAD+
-
native LPD
0.08
NAD+
-
mutant E354K
0.08
NAD+
-
pH 8.0, 37C
0.1 - 0.11
NAD+
-
chloroplastic enzyme
0.11
NAD+
-
mutant H322Y
0.15
NAD+
-
-
0.156
NAD+
-
37C, pH 8.0
0.156
NAD+
-
pH 7.0, 30C, wild-type enzyme
0.16
NAD+
-
mutant enzyme N286Q; mutant N286Q
0.182
NAD+
-
pH 7.0, 30C, mutant enzyme E423A, assay in the absence of KCI
0.186
NAD+
-
pH 7.0, 30C, wild-type enzyme, assay in the absence of KCI
0.19
NAD+
-
mutant W366A, pH 8.0, 37C, presence of 1.5 mM EDTA; wild-type, pH 8.0, 37C, presence of 1.5 mM EDTA
0.199
NAD+
-
pH 7.0, 30C, mutant enzyme E423D
0.203
NAD+
-
pH 7.0, 30C, mutant enzyme E423Q
0.211
NAD+
-
pH 7.0, 30C, mutant enzyme E423S
0.215
NAD+
-
pH 7.0, 30C, mutant enzyme E423A
0.22
NAD+
-
wild-type; wild type enzyme
0.22
NAD+
-
wild-type E3
0.25
NAD+
-
mutant enzyme K37E
0.28
NAD+
-
-
0.28
NAD+
-
mutant T148G
0.288
NAD+
-
pH 7.0, 30C, mutant enzyme E423Q, assay in the absence of KCI
0.29
NAD+
-
mutant T148S
0.292
NAD+
-
pH 7.0, 30C, mutant enzyme E423D, assay in the absence of KCI
0.3
NAD+
-
mutant enzyme N286D; mutant N286D
0.31
NAD+
-
mutant enzyme E192Q
0.312
NAD+
-
pH 7.0, 30C, mutant enzyme E423S, assay in the absence of KCI
0.32
NAD+
-
native enzyme and mutant enzyme E457Q
0.34
NAD+
-
mutant D320N; mutant enzyme D320N
0.38
NAD+
-
mutant enzyme H452Q
0.4
NAD+
-
complex-bound dihydrolipoamide dehydrogenase
0.4
NAD+
-
wild-type enzyme
0.43
NAD+
-
mutant R281K
0.5
NAD+
A5N930
-
0.5
NAD+
-
mutant R281N
0.55
NAD+
-
mutant enzyme S53K/K54S
0.62 - 0.64
NAD+
-
mitochondrial enzyme
0.71
NAD+
A4V929
-
0.82
NAD+
-
recombinant DLDH expressed without without a lipoyl protein domain
0.985
NAD+
-
recombinant DLDH expressed without lipoic acid
1.037
NAD+
-
recombinant DLDH
1.83
NAD+
-
free dihydrolipoamide dehydrogenase
0.00315
NADH
A4V929
-
0.0041
NADH
-
reaction with thio-NAD+
0.0061
NADH
B6F1A8
in 50 mM potassium phosphate buffer (pH 6.0), at 25C
0.0084
NADH
-
reaction with O2
0.0085
NADH
-
NADH:2,6-dichlorophenol indophenol reductase activity
0.009
NADH
-
NADH:NAD+ transhydrogenase activity
0.01
NADH
-
lipoamide dehydrogenase activity
0.01
NADH
-
nitric oxide reduction, pH 7.5
0.021
NADH
-
pH 8.0, 25C, mitochondrial isozyme
0.0215
NADH
-
-
0.023
NADH
-
-
0.038
NADH
A5N930
-
0.04
NADH
-
wild-type; wild type enzyme
0.058
NADH
O81413
-
0.071
NADH
-
mutant enzyme E192Q
0.09
NADH
-
native DiaA
0.13
NADH
-
mutant enzyme S53K/K54S
0.13
NADH
-
mutant enzyme N286D; mutant N286D
0.14
NADH
-
mutant enzyme N286Q; mutant N286Q
0.15
NADH
-
recombinant DiaA
0.156
NADH
-
reaction with 2,6-dimethyl-1,4-benzoquinone
0.161
NADH
-
reaction with 5-hydroxy-1,4-naphthoquinone
0.24
NADH
-
mutant D320N; mutant enzyme D320N
0.25
NADH
A5N930
in diaphorase activity
6.2
NADH
-
reaction with lipoic acid
84
NADH
-
reaction with lipoamide
0.35
NADPH
-
recombinant DiaA
2.6
nicotinamide hypoxanthine dinucleotide
-
-
0.5
Nitro blue tetrazolium
-
recombinant DiaA
0.0005
NO
-
nitric oxide reduction, pH 7.5
0.3
pyruvate
-
mutant E354K
0.4
pyruvate
-
native LPD
0.48
pyruvate
-
mutant H322Y
0.5
R,S-lipoamide
-
-
-
0.42
S-nitroso-N-acetylpenicillamine
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
5.48
S-nitroso-N-acetylpenicillamine
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.12
S-nitrosoglutathione
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.44
S-nitrosoglutathione
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.84
sodium nitroprusside
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37C
2.26
sodium nitroprusside
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.036
thio-NAD+
-
reaction with NADH
0.11
thio-NADH
-
-
2.15
lipoic acid
-
-
additional information
additional information
-
ping pong kinetics
-
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 4C and 25C, respectively
-
additional information
additional information
-
dehydrogenase and oxidase activity kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
108
1,4-benzoquinone
-
-
190
2,6-dimethyl-1,4-benzoquinone
-
pH 7.5, 25C
6
Dihydrolipoamide
-
mutant P325A, pH 8.0, 37C, presence of 1.5 mM EDTA
8.5
Dihydrolipoamide
-
mutant enzyme S53K/K54S
29.7
Dihydrolipoamide
-
mutant enzyme E192Q
107
Dihydrolipoamide
-
mutant D320N; mutant enzyme D320N
116
Dihydrolipoamide
-
mutant enzyme N286Q; mutant N286Q
159
Dihydrolipoamide
-
mutant enzyme N286D; mutant N286D
220
Dihydrolipoamide
-
mutant R281N
223
Dihydrolipoamide
-
mutant R281K
448
Dihydrolipoamide
-
pH 8.0, 25C, mitochondrial isozyme, reverse reaction, varying conditions
505
Dihydrolipoamide
-
wild-type; wild type enzyme
505
Dihydrolipoamide
-
wild-type E3
567
Dihydrolipoamide
-
wild-type enzyme
655
Dihydrolipoamide
-
mutant T148G
742
Dihydrolipoamide
-
mutant T148S
899
Dihydrolipoamide
-
wild-type, pH 8.0, 37C, presence of 1.5 mM EDTA
1032
Dihydrolipoamide
-
mutant W366A, pH 8.0, 37C, presence of 1.5 mM EDTA
220
DL-lipoylpentanoate
-
pH 7.5, 25C
345
H-protein
-
-
-
14.4
Lipoamide
-
mutant enzyme S53K/K54S
23
Lipoamide
-
mutant enzyme K54E
67
Lipoamide
-
mutant D320N; mutant enzyme D320N
81.3
Lipoamide
-
mutant enzyme E192Q
88
Lipoamide
-
-
134
Lipoamide
-
mutant enzyme N286D; mutant N286D
135.5 - 337
Lipoamide
-
pH 8.0, 25C, mitochondrial isozyme, forward reaction, varying conditions
148
Lipoamide
-
mutant enzyme N286Q; mutant N286Q
519
Lipoamide
-
wild-type; wild type enzyme
649
Lipoamide
-
wild-type enzyme
6.75
NAD+
-
mutant enzyme S53K/K54S
30
NAD+
-
mutant enzyme E192Q
135.5 - 337
NAD+
-
pH 8.0, 25C, mitochondrial isozyme, forward reaction, varying conditions
160
NAD+
-
recombinant DLDH
223
NAD+
-
recombinant DLDH expressed without lipoic acid
506
NAD+
-
recombinant DLDH expressed without without a lipoyl protein domain
574
NAD+
-
wild-type enzyme
19.8
NADH
-
mutant enzyme S53K/K54S
26.2
NADH
-
mutant enzyme E192Q
340
NADH
-
wild-type enzyme
448
NADH
-
pH 8.0, 25C, mitochondrial isozyme, reverse reaction, varying conditions
0.25
O2
-
pH 7.5, 25C
190
R,S-lipoamide
-
-
-
72
ubiquinone
-
pH 7.5, 37C, in absence of Zn2+
300
ubiquinone
-
pH 7.5, 37C, in presence of Zn2+
70
lipoic acid
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
turnover numbers for small polypeptides derived from proteolytic treatment of the H-protein
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
Dihydrolipoamide
-
pH 7.0, 30C
0.29
diphenyleneiodonium chloride
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.31
diphenyleneiodonium chloride
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.35
diphenyleneiodonium chloride
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.45
diphenyleneiodonium chloride
-
using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.56
diphenyleneiodonium chloride
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.6
diphenyleneiodonium chloride
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.8
diphenyleneiodonium chloride
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.0488
Lipoamide
-
recombinant DLDH expressed without lipoic acid, in the presence of 4 mM NAD+
0.0566
Lipoamide
-
recombinant DLDH, 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+
0.000865
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
P9WHH8
pH and temperature not specified in the publication
0.001
NADH
-
native pyruvate dehydrogenase complex
0.0044
NADH
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide
0.009
NADH
-
free dihydrolipoamide dehydrogenase
0.0096
NADH
-
mutant H322Y
0.01
NADH
-
mutant E354K
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
0.016
NADH
-
complex-bound dihydrolipoamide dehydrogenase
0.02
NADH
-
chloroplastic enzyme
0.0351
NADH
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 2 mM NAD+
0.0722
NADH
-
recombinant DLDH, in the presence of 2 mM NAD+
0.084
NADH
-
recombinant DLDH expressed without lipoic acid, in the presence of 2 mM NAD+
0.11
NADH
-
mitochondrial enzyme
1.43
valproyl-CoA
-
-
1.6
valproyl-dephosphoCoA
-
-
0.8793
Lipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide
additional information
additional information
-
Zn2+ inhibition kinetics and mechanism
-
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
P9WHH8
pH and temperature not specified in the publication
0.00196
diisopropyl fluorophosphate
-
-
0.59
diphenyleneiodonium chloride
-
using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
0.68
diphenyleneiodonium chloride
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
1.75
diphenyleneiodonium chloride
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
1.81
diphenyleneiodonium chloride
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
1.93
diphenyleneiodonium chloride
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
2.61
diphenyleneiodonium chloride
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
3.31
diphenyleneiodonium chloride
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37C
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
P9WHH8
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
-
purified enzyme in absence of Zn2+
0.05
-
purified enzyme in presence of Zn2+
0.17
Q0KBV8
substrate 5,5'-dithiobis-(2-nitrobenzoic acid), 30C, pH 6.5
0.19
-
substrate 5,5'-dithiobis-(2-nitrobenzoic acid), 30C, pH 6.5
0.344
Q8MUB0
cell lysate, in 50 mM potassium phosphate buffer, pH 6.7, at 37C
0.36
A4V929
purified DLDH
0.5
-
metmyoglobin reduction, in absence of methylene blue, pH 7.5
0.6
-
O2 reduction, pH 6.0
0.8
-
cytochrome c reduction, in absence of methylene blue, pH 7.5
1.7
-
lipoic acid reduction, pH 6.0
2.5
B6F1A8
crude extract, in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25C
3.6
-
pH 7.0, 30C, mutant enzyme E423Q, assay in the absence of KCI
4.5
-
metmyoglobin reduction, in presence of methylene blue, pH 7.5
4.6
-
pH 7.0, 30C, mutant enzyme E423A, assay in the absence of KCI
4.7
Q0KBV8
substrate alpha-lipoic acid, 30C, pH 6.5
4.9
-
pH 7.0, 30C, mutant enzyme E423D, assay in the absence of KCI
5
-
pH 7.0, 30C, mutant enzyme E423S, assay in the absence of KCI
5.6
-
pH 7.0, 30C, wild-type enzyme, assay in the absence of KCI
5.8
-
pH 7.0, 30C, mutant enzyme E423S, assay in the presence of 2 M KCI
6.2
-
pH 7.0, 30C, mutant enzyme E423A, assay in the presence of 2 M KCI
6.4
-
cytochrome c reduction, in presence of methylene blue, pH 7.5
6.4
-
pH 7.0, 30C, mutant enzyme E423Q, assay in the presence of 2 M KCI
6.65
Q8MUB0
19.3fold purified enzyme, in 50 mM potassium phosphate buffer, pH 6.7, at 37C
7.2
-
2,6-dichlorophenolindophenol reduction, pH 6.0
7.8
-
substrate alpha-lipoic acid, 30C, pH 6.5
16.2
-
pH 7.0, 30C, mutant enzyme E423D, assay in the presence of 2 M KCI
16.6
-
purified recombinant mutant D473L
19.1
-
pH 7.0, 30C, wild-type enzyme, assay in the presence of 2 M KCI
20
-
37C, pH 8.0
22.4
-
purified enzyme, at pH 6.5 and 25C
24
-
pH 8.0, 37C
40
Azotobacter agilis
-
-
59.2
B6F1A8
after 23.9fold purification, in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25C
62
-
enzyme from chloroplast
83.06
O81413
lipoamide reduction
90.2
-
-
100
Q0KBV8
substrate alpha-lipoamide, 30C, pH 6.5
110
-
substrate alpha-lipoamide, 30C, pH 6.5
143.1
-
mutant N286Q
154
-
lipoamide reduction, pH 6.0
179.6
-
mutant N286D
210
-
nitric oxide reduction, pH 6.0
280
-
purified recombinant mutant T44V enzyme
283.1
-
mutant D320N
295
-
mitochondrial enzyme
400
-
about, purified recombinant enzyme
586.5
-
wild-type
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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 37C 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
reduction of nitric oxide, lioamide, lipoic acid, and 2,6-dichlorophenolindophenol
5.5
-
optimum in absence of Zn2+
5.8
P09623
monomeric enzyme
6
-
optimum in presence of Zn2+
6.2
-
NADH-lipoamide oxidoreductase activity
6.4
-
reduction of lipoamide
7 - 7.5
Q8NTE1
50 mM phosphate buffer
7 - 7.5
-
assay at
7
-
reaction with NAD(P)H and lipoamide
7
-
reverse reaction, isozyme mLipDH
7
A4V929
NADH:lipoamide oxidoreductase activity
7
-
assay at
7.2
-
NADH-dependent reduction of lipoamide
7.4
-
reduction of 2,6-dichlorophenol indophenol
7.4
-
assay at
7.5
-
reduction of thio-NAD+
7.5
-
reduction of cytochrome c and myoglobin, oxidation of NADH
7.5
-
assay at
7.5
P09623
tetrameric and dimeric enzyme
8
-
dihydrolipoamide-NAD+ oxidoreductase activity
8
-
assay at
8
-
assay at
8.3
-
in the reverse reaction
8.5
-
in the forward reaction
8.5
-
wild-type enzyme and mutant enzymes E423D, E423Q, E423S, and E423A
9
-
reaction with NAD(P)+ and dihydrolipoamide
9
-
forward reaction, isozyme LipDH
additional information
-
highest activity at acidic pH
additional information
-
enzyme prefers acidic pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8
-
-
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 - 8
-
nitric oxide reduction
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 - 7
B6F1A8
high activity in a pH range of 6.0 to 7.0
6 - 8
A5N930
-
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
assay at
30
-
assay at
30
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
55
A4V929
NADH:lipoamide oxidoreductase activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
assays are performed at 4C and at 25C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
Q811C4
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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)
Manually annotated by BRENDA team
-
significant increase in DLDH dehydrogenase activity in rats only for the period between 30 and 60 days of age
Manually annotated by BRENDA team
-
significant increase in DLDH dehydrogenase activity in rats only for the period between 30 and 60 days of age
Manually annotated by BRENDA team
-
increase in DLDH dehydrogenase activity in rats between 10 and 20 days of age, with no further increase evident thereafter
Manually annotated by BRENDA team
Starkeyomyces koorchalomoides
-
-
Manually annotated by BRENDA team
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
Manually annotated by BRENDA team
O81413
enzyme form FlbR-2
Manually annotated by BRENDA team
-
enzyme is not detected on Western blots probed with antibodies that recognize mitochondrial dihydrolipoamide dehydrogenase
Manually annotated by BRENDA team
additional information
-
both genes are transcribed during erythrocytic development of the parasite
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to the matrix, release of enzyme during acrosomal exocytosis
-
Manually annotated by BRENDA team
-
activity is about one-tenth of that in mitochondria
Manually annotated by BRENDA team
-
juxtanuclear localization, like Golgi, in spermatids
Manually annotated by BRENDA team
Starkeyomyces koorchalomoides
-
mitochondrial matrix
Manually annotated by BRENDA team
-
enzyme is part of multienzyme complexes in the inner mitochondrial membrane
Manually annotated by BRENDA team
-
isozyme mLipDH is a component of the branched-chain 2-ketoacid dehydrogenase and the 2-ketoglutarate dehydrogenase multienzyme complexes
Manually annotated by BRENDA team
-
DLDH exclusively exists in mitochondria
Manually annotated by BRENDA team
-
Lpd1 protein is localized in the mitochondria during the logarithmic yeast growth and the filamentous growth
Manually annotated by BRENDA team
Starkeyomyces koorchalomoides FDUS 0337
-
mitochondrial matrix
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
-
-
-
Manually annotated by BRENDA team
-
cytoplasmic surface of plasma membrane
Manually annotated by BRENDA team
Candida albicans CAI4
-
Lpd1 protein is localized in the mitochondria during the logarithmic yeast growth and the filamentous growth
-
Manually annotated by BRENDA team
additional information
-
synthesized predominantly on free ribosomes and translocated into mitochondria
-
Manually annotated by BRENDA team
additional information
-
release of enzyme during acrosomal exocytosis, extramitochondrial localization in epididymal spermatozoa in mammalia
-
Manually annotated by BRENDA team
additional information
-
subcellular localization study using recombinant expression of the isozymes fused to fluorescent protein tags
-
Manually annotated by BRENDA team
additional information
-
no DLDH diaphorase activity in the cytosol
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Neisseria meningitidis serogroup B (strain MC58)
Rhizobium meliloti (strain 1021)
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
-
native protein using SDS-PAGE
702739
24980
-
predicted from cDNA
702739
28000
-
recombinant protein using SDS-PAGE, in good agreement with the calculated molecular weight of recombinant DiaA
702739
43000
-
sequence analysis
690755
50000
Starkeyomyces koorchalomoides
-
SDS-PAGE
711320
50070
-
enzyme including the bound FAD
673190
54000
-
SDS-PAGE
713453
61600
-
full-length recombinant DLDH, sequence analysis
693005
86000
-
native form of recombinant DiaA, gel filtration
702739
88000
-
gel filtration
393966
98000
-
gel filtration
393986
100000
-
equilibrium sedimentation
348939
102000
-
gel filtration
393990
102000
B6F1A8
native enzyme, gel filtration
712521
105000
-
gel filtration
393991
105000
-
gel filtration
394008
107000
A4V929
blue native PAGE
692385
110000
-
gel filtration
348944
110000
-
gel filtration
394009
110000
-
non-denaturing gradient PAGE
486168
110000
-
wild-type and mutants, molecular sieving HPLC
674943
110000
A5N930
gel filtration
691392
110000
-
molecular sieving HPLC
693271
112000
-
gel filtration
393981
115000
-
LPD-Val, gel filtration
393980
115000
-
gel filtration
658231, 658600
117000
-
gel filtration
393984
118000
-
gel filtration
393974
119000
-
gel filtration
393981
120000
-
gel filtration
393981
125000
-
LPD-Glc, gel filtration
393980
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 50000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
Q811C4
x * 56000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 58000, SDS-PAGE
?
-
x * 61000, SDS-PAGE
?
-
x * 59000, SDS-PAGE
?
-
x * 56000, mitochondrial enzyme, SDS-PAGE
?
-
x * 58000, enzyme from heart, SDS-PAGE, x * 56000, enzyme from liver enzyme
?
-
x * 49342, electrospray mass spectrometry
?
-
x * 49757, mitochondrial enzyme, electrospray mass spectrometry
?
-
x * 49690, calculation from nucleotide sequence
?
-
x * 52000, enzyme from chloroplast, SDS-PAGE
?
-
x * 51274, calculation from nucleotide sequence
?
-
x * 52614, enzyme from chloroplast, electrospray mass spectrometry
?
-
? * 50000, SDS-PAGE
?
-
x * 66500, SDS-PAGE
?
-
x * 28206, sequence analysis
?
-
x * 28430, sequence analysis
?
Q9I3D1
x * 57000, SDS-PAGE, His-tagged recombinant protein
?
-
x * 63489, calculated
?
Pseudomonas aeruginosa ATCC 15692
-
x * 57000, SDS-PAGE, His-tagged recombinant protein
-
?
-
x * 63489, calculated
-
?
Haloferax volcanii DSM 3757
-
x * 66500, SDS-PAGE
-
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
x * 46000, SDS-PAGE
dimer
-
2 * 55000
dimer
O81413
x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis
dimer
-
2 * 50216, amino acid sequence calculation
dimer
-
2 * 55000, about, SDS-PAGE
dimer
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
dimer
P09623
2 * 52000, present at pH 5.8 and 7.5, active at pH 7.5
dimer
A5N930
2 * 50000, SDS-PAGE, 2 * 53000, sequence analysis
dimer
-
molecular sieving HPLC
dimer
-
wild-type and mutants, molecular sieving HPLC
dimer
Synechocystis sp. PCC6803
-
2 * 55000, SDS-PAGE
-
homodimer
-
-
homodimer
B6F1A8
2 * 50000, SDS-PAGE
homodimer
-
2 * 55000, SDS-PAGE
homodimer
-
x-ray crystallography
homodimer
A4V929
2 * 45400, sequence analysis, 2 * 45000, SDS-PAGE
homodimer
B6F1A8
2 * 49912, calculated from amino acid sequence
homodimer
Microbacterium luteolum JCM 9174
-
2 * 50000, SDS-PAGE, 2 * 49912, calculated from amino acid sequence
-
tetramer
P09623
present at pH 5.8 and 7.5, active at pH 7.5
trimer
-
gel filtration, 3 * 28000 Da
monomer
P09623
1 * 54000, only present and active at pH 5.8
additional information
-
-
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
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 oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions
additional information
-
2 distinct dihydrolipoamide dehydrogenases, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
additional information
Q811C4
the enzyme is the E3 component of 2-keto acid dehydrogenase multienzyme complex
additional information
-
the homodimeric enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
Q811C4
tyrosine-phosphorylated
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
additional information
-
the apicoplast isozyme contains a potential transit peptide, the mitochondrial isozyme contains targeting sequence
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
-
hanging drop vapour diffusion method
-
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
P9WHH8
hanging drop vapour diffusion method
P9WHH9
crystallization by dialysis
-
best results obtained by vapour diffusion method, three-dimensional structure at 2.8 A resolution
-
crystallized by hanging-drop vapor-diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
enzyme loses its activity completely below pH 6 and above pH 11
702739
6 - 9
A5N930
retains about half of the initial activity
691392
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
recombinant enzyme is stable at 30C upon 30 min of incubation without substrates, but incubation at 40C and higher temperatures inactivated enzyme activity
702739
55 - 70
B6F1A8
the remaining activity after thermal treatment at pH 7.0 for 15 min is 90% at 55C, 80% at 60C, 70% at 65 C, and 45% at 70C
712521
60
A5N930
the enzyme maintains some activity after a 30-min incubation
691392
65
-
170 min, 50% loss of activity
393990
65
-
the enzyme unfolds irreversibly at heat treatment higher than 65C
674368
70
-
50 min, 50% loss of activity
393990
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
393990
80
-
6 min, 50% loss of activity
393990
86
-
melting temperature
393973
95
-
15 min, in presence of 4 M NaCl, enzyme in crude extract, stable
393981
100
-
inactivated by boiling, enzyme in crude extract
393981
additional information
-
-
392950
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 20C 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 16-18C lower than in the presence of salt
727409
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to trypsin treatment
-
no loss of activity when the enzyme is frozen at -20C, and thawed three times
Q8NTE1
trypsin or papain, treatment with 0.019 mg/ml protease
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 6 months
-
-20C, stable for several months
-
-20C, 6 months, about 60% loss of activity
-
4C, 3 months
A5N930
4C or -20C, stable for at least 1 month
Q8NTE1
stable for months if stored in liquid nitrogen
-
-20C, 6 months, about 10% loss of activity
-
purified recombinant enzyme, -20C, 100 mM potassium phosphate, 100 mM KCl, pH 7.0, 1 mM EDTA, 50% v/v glycerol, stable for at least 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
-
from pyruvate dehydrogenase complex
-
from pyruvate dehydrogenase complex
-
Ni-NTA column chromatography
Q8MUB0
by gel filtration
A5N930
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
-
purified from strain ASKA clone (-) JW0112
B1IQM4
gel filtration
-
HiTrap Q column chromatography
-
-
O81413
purified using copper-based metal ion affinity chromatography in the presence of 2 M KCl
-
gel filtration; wild-type and mutant proteins, highly purified
-
Ni-NTA agarose column chromatography, gel filtration
-
Ni-NTA resin column chromatography and gel filtration
-
nickel iminodiacetic acid Sepharose 6B column chromatography
-
recombinant D473L mutant from Escherichia coli to homogeneity
-
recombinant His-tagged E3 wild-type and mutant proteins
-
recombinant mutant T44V from Escherichia coli strain XL1-Blue
-
Sephacryl S-100 column gel filtration
-
Strep-Tactin Sepharose column chromatography
-
Superdex HR-200 gel filtration
-
wild-type and mutant enzymes K37E, H452Q and E457Q
-
wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q
-
wild-type DLD and mutants purified by nickel affinity chromatography. C-term DLD purified to near homogeneity by a five-step procedure
-
DEAE-Toyopearl 650 M column chromatography, butyl-Toyopearl 650 M column chromatography, and TSK-gel G3000SW gel filtration
B6F1A8
by gel filtration
-
metal-affinity chromatography and Superdex 200 gel filtration chromatography
P9WHH9
Ni-NTA-agarose resin column chromatography and Superdex 200 gel filtration
P9WHH8
recombinant enzyme
-
recombinant His-tagged truncated isozymes from Escherichia coli by nickel affinity chromatography to 98% homogeneity
-
dissociation of the lipoamide dehydrogenase component from the branched-chain alpha-keto acid dehydrogenase complex during purification
-
gel filtration
-
presence of dithiothreitol during purification preserves enzymatic activity
-
affinity chromatography on propyllipoamide-glass columns
-
from pyruvate dehydrogenase complex
-
ammonium sulfate precipitation and Ni-NTA agarose column chromatography
Starkeyomyces koorchalomoides
-
gel filtration, at least 90% pure
-
ammonium sulfate precipitation
-
affinity chromatography on propyllipoamide-glass columns
-
further purification of the commercial preparation
-
further purification of the commercial preparation by gel filtration
-
partially
-
Sephadex G-25 column gel filtration
P09623
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
into vector pET101/D TOPO and expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
Q8MUB0
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)
A5N930
expressed in Escherichia coli as a recombinant protein
-
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
Q8NTE1
expression in Escherichia coli
Q0KBV8
expressed in Escherichia coli BL21(DE3)
B1IQM4
expressed in Escherichia coli M109(lambdaDE3)
-
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex, expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)
P11959
overexpression in Escherichia coli
O81413
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
-
expression in a strain of Haloferax volcanii lacking dihydrolipoamide dehydrogenase activity
-
overexpressed in the parent organism by using the halophilic archaeal rRNA promoter
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli JM83 cells
-
expressed in Escherichia coli XL1-Blue
-
expressed in Escherichia coli; His-tagged wild-type and mutant proteins overexpressed in Escherichia coli
-
expression of D473L mutant in Escherichia coli strain XL1-Blue
-
expression of mutant T44V in Escherichia coli strain XL1-Blue
-
mutants cloned into pQE-9 vector
-
wild-type and mutant enzymes K37E, H452Q and E457Q; wild-type and mutant enzymes K37E, H452Q and E457Q, overexpression in Escherichia coli
-
wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q, overexpression in Escherichia coli
-
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
-
expressed in Escherichia coli JM109 cells
B6F1A8
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
-
expressed in Escherichia coli
P9WHH9
expressed in Escherichia coli BL21(DE3) Codon Plus RLI cells
P9WHH8
expression in Escherichia coli
-
Mycobacterium smegmatis over-expressing LpdC protein
-
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
-
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
-
expressed in Escherichia coli
Starkeyomyces koorchalomoides
-
expressed in Escherichia coli BL21(DE3)
Q8VPK7
expressed in Escherichia coli M15 cells
-
expressed in Escherichia coli M15pREP4 cells
-
expressed in Escherichia coli strain JRG 1342
-
expression in Escherichia coli strain JRG 1342
-
expressed in Escherichia coli BL21(DE3)
P50970
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
-
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
-
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 20C 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
Haloferax volcanii DSM 3757
-
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
Haloferax volcanii DSM 3757
-
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 20C lower than the wild-type
-
E423Q
Haloferax volcanii DSM 3757
-
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
Haloferax volcanii DSM 3757
-
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
-
A1444G
-
substitution located in exon 13 leading to 20% of wild type activity
C45S
-
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
-
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
-
missense mutation, expressed at 28C the mutant exhibits essentially wild-type E3 activity, at 37C the activity is reduced to 12% of that of the wild type enzyme
D444V
-
pathogenic mutation, diminishing the ability of E3 to homodimerize
D444V
-
shows weak proteolytic activity with mature frataxin substrate, but consistently cleaves mature frataxin to denoted frataxin products with faster kinetics than the wild-type
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
-
missense mutation, expressed at 28C the mutant exhibits essentially wild-type E3 activity, at 37C the activity is reduced to 38% of that of the wild type enzyme
E340K
-
pathogenic mutation, diminishing the ability of E3 to homodimerize
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
G194C
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
H348A
-
the mutant shows 60% activity in the forward reaction and 66% activity in the reverse reaction compared to the wild type enzyme
H348L
-
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
I358T
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
I51A
-
mutant with about 100fold reduced activity compared to the wild type enzyme
K37E
-
molar ratio of FAD to enzyme is 0.76 compared to 1 for the wild-type enzyme
K37E
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
K54E
-
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
P453L
-
causes E3 deficiency
P453V
-
1650fold lower specific activity compared to the wild type enzyme
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 28C the mutant exhibits essentially wild-type E3 activity, at 37C the activity is reduced to 28% of that of the wild type enzyme
R460G
-
missense mutation, the dissociation constant is three orders of magnitude higher than that of wild-type E3
R460G
-
pathogenic mutation, diminishing the ability of E3 to homodimerize
S456A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
S456A/D444V
-
low levels of residual 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
-
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
-
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
-
mutation of highly conserved residue. kinetic parameters similar to wild-type
Y438A
-
the mutant shows 100% activity in the forward reaction and 91% activity in the reverse reaction compared to the wild type enzyme
Y438F
-
the mutant shows 100% activity in the forward reaction and 112% activity in the reverse reaction compared to the wild type enzyme
Y438H
-
the mutant shows 99% activity in the forward reaction and 92% activity in the reverse reaction compared to the wild type enzyme
A181V
P9WHH8
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
P9WHH8
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
D5A
P9WHH9
4.3% activity of the wild type enzyme
E91A
P9WHH9
49.6% activity of the wild type enzyme
E91K
P9WHH9
62.5% activity of the wild type enzyme
F269R
P9WHH8
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
F464A
P9WHH9
5% activity of the wild type enzyme
G312A/L313G/L314P/Q315M
P9WHH8
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
H386A
P9WHH9
20% activity of the wild type enzyme
H386K
P9WHH9
9% activity of the wild type enzyme
H460E
P9WHH9
69.4% activity of the wild type enzyme
H98A
P9WHH9
3.3% activity of the wild type enzyme
K103E
P9WHH9
17.7% activity of the wild type enzyme
K105A
P9WHH9
44.7% activity of the wild type enzyme
K216A
P9WHH9
58.3% activity of the wild type enzyme
K220A
P9WHH9
81.2% activity of the wild type enzyme
K223A
P9WHH9
67.1% activity of the wild type enzyme
K223E
P9WHH9
70.5% activity of the wild type enzyme
K224A
P9WHH9
55.2% activity of the wild type enzyme
K376A
P9WHH9
52.2% activity of the wild type enzyme
K67A
P9WHH9
67.3% activity of the wild type enzyme
K67E
P9WHH9
64.3% activity of the wild type enzyme
K88E
P9WHH9
74.8% activity of the wild type enzyme
L314P
P9WHH8
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
P9WHH8
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
N43A
P9WHH9
11% activity of the wild type enzyme
R147T
P9WHH8
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
P9WHH8
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
R93A
P9WHH9
6.5% activity of the wild type enzyme
R93E
P9WHH9
3.6% activity of 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
-
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
-
K43A
-
unable to express the mutant protein
M326V
-
mutation affecting the ability of FAD, NAD+, or NADH to bind to E3
additional information
-
deletion mutant DELTAG101 causes E3 deficiency
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
-
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
K43R
-
expresses well, but still has lipoic acid attached
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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inactivation of the enzyme by guanidine-HCl is reversible by its removal
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
P11959
shows NADH-dependent tellurite reductase activity in vitro
degradation
-
conservation of the Cys-45 residue in human E3 is essential to the efficient catalytic function of the enzyme
degradation
-
N286 and D320 play a role in the catalytic function of the 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
degradation
-
T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3
medicine
-
mutations of the enzyme cause the often-fatal human disease known as E3 deficiency
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 Alzheimers disease
degradation
-
DLD is required for hamster acrosome reaction
degradation
-
shows strong diaphorase activity
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
medicine
Mus musculus C57/Bl-6
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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
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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
Q9I3D1
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
Pseudomonas aeruginosa ATCC 15692
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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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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
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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
medicine
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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
degradation
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shows flavin reductase activity with moderate diaphorase activity
medicine
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dihydrolipoyl dehydrogenase is an important source of reactive oxygen species leading to life span limitation
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
degradation
P50970
shows NADH-dependent tellurite reductase activity in vitro
additional information
A4V929
metabolic context(s) of DLDHs remains an open question
degradation
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shows NADH-dependent tellurite reductase activity in vitro
additional information
A5N930
high stability of rBfmBC may make it useful for practical use
degradation
B1IQM4
shows NADH-dependent tellurite reductase activity in vitro
additional information
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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
degradation
Q8VPK7
shows NADH-dependent tellurite reductase activity in vitro
additional information
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the lipoyl protein domain (but not lipoic acid alone) plays a regulatory role in the enzymatic characteristics of pneumococcal DLDH