1.8.1.4: dihydrolipoyl dehydrogenase
This is an abbreviated version!
For detailed information about dihydrolipoyl dehydrogenase, go to the full flat file.
Word Map on EC 1.8.1.4
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1.8.1.4
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multienzyme
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fad
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acetyltransferase
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dehydrogenases
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alpha-ketoglutarate
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flavin
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branched-chain
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flavoproteins
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transacetylase
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thioredoxin
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azotobacter
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vinelandii
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thiamin
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subcomplexes
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alpha-keto
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acidosis
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alpha-ketoacids
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succinyltransferase
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mercuric
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flavoenzymes
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2-oxoacids
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trypanothione
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friedreich
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1.2.4.1
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subunit-binding
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two-electron
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radiofrequency
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medicine
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ketoacids
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degradation
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ashkenazi
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t-proteins
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myenteric
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analysis
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drug development
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diagnostics
- 1.8.1.4
-
multienzyme
- fad
- acetyltransferase
- dehydrogenases
- alpha-ketoglutarate
- flavin
-
branched-chain
- flavoproteins
- transacetylase
- thioredoxin
-
azotobacter
- vinelandii
- thiamin
-
subcomplexes
-
alpha-keto
- acidosis
- alpha-ketoacids
- succinyltransferase
-
mercuric
-
flavoenzymes
- 2-oxoacids
- trypanothione
- friedreich
-
1.2.4.1
-
subunit-binding
-
two-electron
-
radiofrequency
- medicine
-
ketoacids
- degradation
-
ashkenazi
-
t-proteins
-
myenteric
- analysis
- drug development
- diagnostics
Reaction
Synonyms
apicoplast E3, CDS, CIP50, coronin-interacting protein, dehydrogenase, lipoamide, dehydrolipoate dehydrogenase, DHLDH, DHLipDH, diaphorase, dihydrolipoamide dehydrogenase, dihydrolipoamide dehydrogenase E3, dihydrolipoamide:NAD+ oxidoreductase, dihydrolipoic dehydrogenase, dihydrolipomide dehydrogenase, dihydrolipoyl dehydrogenase, DLD, DLD1, Dld2, DLDH, DLDH dehydrogenase, DLDH diaphorase, DLDH2, DT-diaphorase, E3, E3 component, E3 component of 2-oxoglutarate dehydrogenase complex, E3 component of acetoin cleaving system, E3 component of alpha keto acid dehydrogenase complexes, E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes, E3 component of pyruvate complex, E3 lipoamide dehydrogenase, E3 protein component of 2-oxoacid dehydrogenase multienzyme complexes, E3 subunit of the alpha-ketoglutarate dehydrogenase complex, EC 1.6.4.3, Glycine cleavage system L protein, Glycine oxidation system L-factor, hDLDH, hE3, hLADH, L-protein, LAD, LADH, LDH, LDP-Glc, LDP-Val, LipDH, lipoamide dehydrogenase, lipoamide dehydrogenase (NADH), lipoamide dehydrogenase C, lipoamide dehydrogenase2, lipoamide oxidoreductase (NADH), lipoamide reductase, lipoamide-dehydrogenase-valine, lipoate dehydrogenase, lipoic acid dehydrogenase, lipoyl dehydrogenase, LPD, LPD-GLC, LPD-VAL, LPD1, LPD2, Lpd3, LpdA, LpdC, LpdG, LpdV, More, mtLPD2, NAD(P)H:lipoamide oxidoreductase, NADH dehydrogenase, NADH diaphorase, NADH:lipoamide oxidoreductase, nicotinamide adenine dinucleotide diaphorase, ORF-E3, pdhD, pdhL, PfaE3, rhDLDH, TAase, ubiquinone reductase
ECTree
1.8.1.4 dihydrolipoyl dehydrogenaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrated DNA + NAD(P)H
?
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enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination which can cause cancer, enzyme might be resonsible for reversing biological nitration processes
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-
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
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enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination
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-
?
protein N6-(dihydrolipoyl)lysine + NAD+
protein N6-(lipoyl)lysine + NADH + H+
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-
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?
reduced lipoamide + NAD+
oxidized lipoamide + NADH
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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
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r
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
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reaction is important to protect the cell e.g. from oxidative stress
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-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
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-
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?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
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-
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?
dihydrolipoamide + NAD+
lipoamide + NADH
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regulation of activity dependent on tyrosine-phosphorylation of the enzyme
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r
dihydrolipoamide + NAD+
lipoamide + NADH
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the forward reaction is the physiological one
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-
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
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-
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r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
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-
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r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
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-
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r
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
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?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
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-
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
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-
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r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
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-
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r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
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r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
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-
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r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
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-
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r
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
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enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
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-
?
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
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-
?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
-
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
-
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
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the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
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-
?
additional information
?
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the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
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-
?
additional information
?
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the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
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-
?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
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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
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?
additional information
?
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enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosphorylation, overview
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?
additional information
?
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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
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-
?
additional information
?
-
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
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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
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-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
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-
LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase
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-
?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
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lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
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?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
additional information
?
-
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the enzyme might play a role in modifying NO levels under specific cell conditions
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?
additional information
?
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the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system
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?
