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Enzyme Nomenclature
Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
for references in articles please use BRENDA:EC1.8.1.4
Word Map on EC 1.8.1.4
- 1.8.1.4
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multienzyme
- fad
- disulfide
- alpha-ketoglutarate
- flavin
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branched-chain
- flavoproteins
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transacetylase
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azotobacter
- vinelandii
- thioredoxin
- acidosis
- thiamin
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subcomplexes
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alpha-keto
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flavoenzymes
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mercuric
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alpha-ketoacids
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succinyltransferase
- 2-oxoacids
- trypanothione
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two-electron
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subunit-binding
- friedreich
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fad-binding
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t-proteins
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ashkenazi
- medicine
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ketoacids
- protochlorophyllide
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frontotemporal
- degradation
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1.2.4.1
- diagnostics
- drug development
- analysis
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.1.4
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RECOMMENDED NAME
GeneOntology No.
dihydrolipoyl dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
involvement of a reversibly reducible disulfide bond in catalytic mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
the mitochondrial isozyme shows ping pong kinetic mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
formation of a FADH2-NAD+ intermediate in catalysis, reaction mechanism of reductive and oxidative half-reactions involving enzyme, FAD/FADH2, and NAD+/NADH
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron-reduced enzyme, both redox centers are reduced, mechanism of the diaphorase reaction which occurs when the enzyme is in the four-electron-reduced state
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
Asp473 is important for efficient catalytic function of the enzyme
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping pong mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Dihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Dihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the physiological direction, dihydrolipoamide, which is covalently tethered to another enzymatic subunit in the multienzyme complex, binds to the disulfide-exchange site near the si face of the FAD cofactor. Ddihydrolipoamide is thought to donate a hydride to the disulfide and a proton to an active-site base forming a stable charge-transfer complex between the thiolate of the mixed disulfide and the oxidized FAD cofactor. In the presence of NAD+, electrons are passed to FAD and then to NAD+ on the re face of the flavin, forming NADH with the release of a proton, mechanism modelling, detailed overview
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
kinetic mechanism of human E3 enzyme is a ping-pong mechanism. In human E3, dihydrolipoamide binds to the si-face of FAD, whereas NAD+ binds to the re-face. These two spatially separate substrate binding sites can allow the enzyme to form a ternary complex with two substrates, which is an essential feature of the sequential mechanism
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protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
oxidation
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oxidation
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catalyzes reoxidation of reduced lipoate attached to H-protein, a lipoic acid-containing protein
reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [6].
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CAS REGISTRY NUMBER
COMMENTARY
9001-18-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex
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diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex; K-12
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dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex
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393971, 393993, 394003, 394004, 658466, 659099, 659101, 672869, 673943, 674382, 674759, 675350, 677161, 691569, 694356, 694854, 711099, 724686, 741757
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UniProt
3D7, 2 lipdh genes encoding 2 isozymes in mitochondrion and apicoplast, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
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dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
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E3 belongs to the pyridine nucleotide-disulfide oxidoreductase family along with glutathione reductase (GR), thioredoxin reductase, mercuric reductase and trypanothione reductase
evolution
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residue Cys50 is absolutely conserved, Cys50 is a component of the very long a-helix structure 2, which is composed of 25 amino acids. Residue Cys50 forms an active disulfide center with Cys45
evolution
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residue H329 is absolutely conserved, H329 329 is a part of the long alpha-helix 8, which is composed of 16 amino acids and is a component of the central domain. His329 is also located near FAD and the active disulfide center between Cys45 and Cys50, which are essential to the catalytic activity of human E3
malfunction
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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
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enhanced arsenate and arsenite sensitivity is due to the disruption of the plastidial LPD1 and LPD2 genes
malfunction
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pathogenic mutations of LADH cause severe metabolic disturbances, called E3 deficiency that often involve cardiological and neurological symptoms and premature death. Some of the known pathogenic mutations augment the reactive oxygen species (ROS) generation capacity of LADH, which may contribute to the clinical presentations. Structural changes are likely to turn the physiological LADH conformation to its ROS-generating conformation
malfunction
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pathogenic mutations of hLADH cause severe metabolic diseases (atypical forms of E3 deficiency) that often escalate to cardiological or neurological presentations and even premature death. The pathologies are generally accompanied by lactic acidosis. hLADH presents a distinct conformation under acidosis (pH 5.5-6.8) with lower physiological activity and the capacity of generating reactive oxygen species (ROS). Molecular dynamics simulation of the structural changes induced in the low-pH conformation of hLADH by five pathogenic mutations of hLADH. Determination of structures of these disease-causing mutants of hLADH, overview
malfunction
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pathogenic amino acid substitutions of the common E3 component (hE3) of the human 2-oxoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause premature death. Determination of structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase involved in E3 deficiency, using hydrogen/deuterium-exchange mass spectrometry
malfunction
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Pfae3 is deleted from Plasmodium falciparum and although the mutants are viable, they display a highly synchronous growth phenotype during intra-erythrocytic development. The mutants also show changes in the expression of some mitochondrial and antioxidant proteins suggesting that deletion of Pfae3 impacts on the parasite's metabolic function with downstream effects on the parasite's redox homoeostasis and cell cycle
malfunction
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as a common component in three 2-oxo acid dehydrogenase, a decrease in E3 activity affects the activities of all three complexes, which leads to increased urinary excretion of 2-oxo acids, elevated blood lactate, pyruvate, and branched chain amino acids. Patients with an E3 deficiency normally die young because an E3 deficiency is a critical genetic defect affecting the central nervous system. A deficiency in E3 results in Leigh syndrome with recurrent episodes of hypoglycemia and ataxia, permanent lactic acidaemia, and mental retardation. A C45A mutation results in a large decrease in human E3 activity and changes in the spectroscopic properties of human E3
malfunction
metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial lipoamide dehydrogenase2. Both arsenate and arsenite inhibit root elongation, decreased seedling size and increase anthocyanin production more profoundly in knockout mutants than in wild-type seedlings, arsenite seems to be the mediator of the observed phenotypes
malfunction
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the homozygous deletion mutant lpd1/lpd1 is unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibits a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5 mM of hydrogen peroxide and shows filamentation defects
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metabolism
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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
metabolism
dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxoglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions
metabolism
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dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxoglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions
metabolism
dihydrolipoamide dehydrogenase (E3) is a component of three different catabolic multienzyme complexes that oxidize pyruvate, 2-oxooglutarate, or glycine, where E3 catalyzes the final step in a sequence of oxidative reactions
physiological function
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effects of insulin treatment on HuC/HuD myoenteric neurons, NADH diaphorase, and nNOS-positive myoenteric neurons of the duodenum of adult rats with acute diabetes is investigated: The density of NADH diaphorase-positive neurons in animals from the diabetic group and in the insulin treated diabetic group is greater than in the control group, indicating that short-term diabetes increases the activity of respiratory chain enzymes
physiological function
Starkeyomyces koorchalomoides
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the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
physiological function
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dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
physiological function
LPD is a useful biocatalyst for regenerating NAD+
physiological function
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plastidial LPD expression quantitatively controls Arabidopsis arsenate sensitivity
physiological function
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dihydrolipoamide dehydrogenase is a FAD-linked subunit of 2-oxooglutarate, pyruvate and branched-chain amino acid dehydrogenases and the glycine cleavage system, transfering electrons from the dihydrolipoic acid prosthetic group to the NAD+ cofactor via its FAD center
physiological function
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lipoamide dehydrogenase-deficient Mycobacterium tuberculosis is severely attenuated in wild type and immunodeficient mice. When dihydrolipoamide acyltransferase is absent, Mycobacterium tuberculosis upregulates an lipoamide dehydrogenase-dependent branched chain keto-acid dehydrogenase encoded by pdhA, pdhB, pdhC and lpdC. Without lipoamide dehydrogenase, Mycobacterium tuberculosis cannot metabolize branched chain amino acids and potentially toxic branched chain intermediates accumulate. Mycobacterium tuberculosis deficient in both dihydrolipoamide acyltransferase and pdhC phenocopies lipoamide Mycobycterium tuberculosis
physiological function
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like the raffinose ATP-binding protein RafK, the presence of the enzyme also activates the expression of raf operon genes. Enzyme-negative pneumococci show a significantly decreased expression of aga and rafEFG, but dihydrolipoamide dehydrogenase does not regulate rafK or the putative regulatory genes rafR and rafS. Dihydrolipoamide dehydrogenase also binds directly to RafK both in vitro and in vivo, indicating the possibility that dihydrolipoamide dehydrogenase regulates raffinose transport by a direct interaction with the regulatory domain of the transporter
physiological function
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
physiological function
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RNA interference or the deletion of both alleles of lipoamide dehydrogenase in bloodstream Trypanosoma brucei results in an absolute requirement for exogenous thymidine. In the absence of thymidine, lipdh-/- parasites show a severely altered morphology and cell cycle distribution. Lipdh-/- cells are unable to infect mice. Degradation of branched-chain amino acids takes place but is dispensable. In cultured bloodstream - but not procyclic - African trypanosomes, the total cellular concentration of lipoamide dehydrogenase increases with increasing cell densities. In procyclic parasites, lipoamide dehydrogenasemRNA depletion causes an even stronger proliferation defect that is not reversed by presence of thymidine
physiological function
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dihydrolipoamide dehydrogenase is a component in the pyruvate-, 2-oxooglutarate- and branched-chain oxoacid dehydrogenase complexes and in the glycine cleavage system
physiological function
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human dihydrolipoamide dehydrogenase is a flavoenzyme component (E3) of the human 2-oxoglutarate dehydrogenase complex and few other dehydrogenase complexes
physiological function
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the enzyme, as the E3 component of the pyruvate decarboxylase complex, has reactive oxygen species generating activity
physiological function
in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview
physiological function
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in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview
physiological function
in vivo, the dihydrolipoamide dehydrogenase component (E3) is associated with the pyruvate, 2-oxoglutarate, and glycine dehydrogenase complexes. The pyruvate dehydrogenase (PDH) complex connects the glycolytic flux to the tricarboxylic acid cycle and is central to the regulation of primary metabolism. Regulation of PDH via regulation of the E3 component by the NAD+/NADH ratio represents one of the important physiological control mechanisms of PDH activity. Steady-state distributions of enzyme redox states as a function of lipoamide/ dihydrolipoamide, NAD+/NADH, and pH, modelling, overview
physiological function
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pyruvate dehydrogenase complex, PDC, is a multi-enzyme complex comprising an E1, pyruvate decarboxylase, an E2, dihydrolipomide acetyltransferase, and an E3, dihydrolipoamide dehydrogenase. Plasmodium PDC is essential for parasite survival in the mosquito vector and for late liver stage development in the human host
physiological function
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E3 catalyzes the reoxidation of the dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of these dehydrogenase complexes
physiological function
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dihydrolipoamide dehydrogenase of Escherichia coli is a bacterial enzyme that is involved in the central metabolism and shared in common between the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. The presence of oligomeric forms of the enzyme is determined by the multifunctionality of LpD in the cell, in particular, the required stoichiometry in the complexes. The E3 enzyme activity is essential for aerobic respiration. Dihydrolipoamide dehydrogenase plays an equally important role in anaerobic organisms, since this enzyme is involved in the synthesis of branched-chain keto and amino acids
physiological function
LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase; LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase; LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase
physiological function
dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD. Since this reaction is the final step of a series of catalytic reaction of pyruvate dehydrogenase multi-enzyme complex (PDC), LipDH is a key enzyme to maintain the fluent metabolic flow
physiological function
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E3 is an essential component in pyruvate, 2-oxoglutarate and branched-chain 2-oxo acid dehydrogenase complexes. E3 catalyzes the reoxidation of a dihydrolipoyl prosthetic group attached to the lysyl residue(s) of the acyltransferase components of the three 2-oxo acid dehydrogenase complexes
physiological function
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the enzyme DLDH shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of hDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations. Native DLDH is tethered to the pyruvate dehydrogenase complex by interactions with a mediatory protein, E3 binding protein (E3BP), via a region that overlaps with the putative TiO2?binding site, involving V347, H348, D413, E437, Y438, G439, E443, D444, and R447
physiological function
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the enzyme shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of rhDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations
physiological function
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dihydrolipoamide dehydrogenase is the E3 subunit of the mitochondrial pyruvate dehydrogenase complex, rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3
physiological function
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dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
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physiological function
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LPD is a useful biocatalyst for regenerating NAD+
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physiological function
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enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
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physiological function
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LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase; LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase; LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase
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physiological function
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the enzyme shows titanium dioxide (TiO2) binding capability. The putative TiO2-binding regions of both the bacterial and human enzymes are found to contain a CHED (Cys, His, Glu, Asp) motif, which has been shown to participate in metal-binding sites in proteins. The binding of rhDLDH to TiO2 at physiological pH values and above is nonelectrostatic and involves chelating/coordinative interactions of DLDH acidic residues with the oxide, docking calculations
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physiological function
Starkeyomyces koorchalomoides FDUS 0337
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the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
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additional information
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molecular dynamics simulation the conformation of enzyme LADH that is proposed to be compatible with the reactive oxygen species (ROS) generation
additional information
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a homology model for PfaE3 reveals an extra anti-parallel beta-strand at the position where human E3BP (E3-binding protein) interacts with E3, a parasite-specific feature that may be exploitable for drug discovery against PDC. E3 enzyme homology structure modelling using the human enzyme structure, PDB ID 2F5Z
additional information
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residue Ala328 is absolutely conserved, suggesting that it might be important for the structure and function of human E3. Ala328 is a component of alpha-helix 8 and is located near the presumed dihydrolipoamide binding channel. Ala328 is also located close to the active disulfide center between Cys45 and Cys50
additional information
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all of the E3 enzymes function as dimers, and their active site contains the reactive disulfide bridge, which is directly involved in catalysis
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity
additional information
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location of residues Pro156 and Pro303 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
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location of residue Cys50 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
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location of residue H329 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
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structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template
additional information
mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis thaliana
additional information
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purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful; purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
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additional information
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structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
cytochrome c is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
2,6-dimethoxy-1,4-benzoquinone + NADH
? + NAD+
8.0% activity compared to lipoamide
-
-
?
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
-
-
-
?
2-hydroxy-1,4-benzoquinone + NADH
2-hydroxy-1,4-benzoquinol + NAD+
-
-
-
-
?
2-methyl-1,4-benzoquinone + NADH
2-methyl-1,4-benzoquinol + NAD+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADH
5-hydroxy-1,4-naphthoquinol + NAD+
-
-
-
-
?
5-nitroblue tetrazolium chloride + NADH
? + NAD+
-
5.1% of the activity with lipoamide
-
-
?
benzyl viologen + NADH
? + NAD+
-
2.9% of the activity with lipoamide
-
-
?
DL-lipoylpentanoate + NADH
? + NAD+
-
100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state
-
-
?
ferrocene + NADH
? + NAD+
3.6% activity compared to lipoamide
-
-
?
ferrocenecarboxylic acid + NADH
? + NAD+
4.1% activity compared to lipoamide
-
-
?
iodonitrotetrazolium chloride + NADH
? + NAD+
19.3% activity compared to lipoamide
-
-
?
lipoamide + 3-acetylpyridine adenine dinucleotide
dihydrolipoamide + ?
-
-
-
-
?
lipoamide + nicotinamide hypoxanthine dinucleotide
dihydrolipoamide + ?
-
-
-
-
?
metmyoglobin + NADH
reduced myoglobin + NAD+
-
myoglobin is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
nitrated DNA + NAD(P)H
?
-
enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination which can cause cancer, enzyme might be resonsible for reversing biological nitration processes
-
-
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
-
enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination
-
-
?
nitrotetrazolium blue + NADH
? + NAD+
2.9% activity compared to lipoamide
-
-
?
pyocyanin + NADH + H
reduced pyocyanin + NAD+
pyocyanin is reported to stimulate respiration
-
-
?
reduced DL-lipoamide + NAD+
oxidized DL-lipoamide + NADH
-
-
-
-
r
resazurin + NADH
? + NAD+
155.8% activity compared to lipoamide
-
-
?
resorufin + NADH
? + NAD+
19.1% activity compared to lipoamide
-
-
?
sulfonated tetrazolium + NADH
? + NAD+
39.2% activity compared to lipoamide
-
-
?
1-methoxyphenazinium methosulfate + NADH
? + NAD+
248.1% activity compared to lipoamide
-
-
?
1-methoxyphenazinium methosulfate + NADH
? + NAD+
248.1% activity compared to lipoamide
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
31.1% of the activity with lipoamide
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
-
-
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
-
90fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
-
-
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
-
-
-
-
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
-
-
-
-
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
-
-
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
-
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
-
-
-
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
-
-
-
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
-
-
-
-
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
Starkeyomyces koorchalomoides FDUS 0337
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
-
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
-
-
?
dihydrolipoamide + NAD
lipoamide + NADH + H+
dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
DLDH activity, forward reaction
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
mutant enzymes C44S and C49S show minute activity
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
the forward reaction is the physiological one
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
-
-
-
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
alternate oxidation and reduction of an intrachain disulfide bond
-
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
specific substrate
-
-
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
specific substrate
-
-
?
lipoamide + NADH
dihydrolipoamide + NAD+
NADH:lipoamide oxidoreductase activity, reverse reaction
-
-
r
lipoamide + NADH
dihydrolipoamide + NAD+
100% activity
-
-
?
mature frataxin + NADH
denoted frataxin + NAD+
-
exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity
-
-
?
menadione + NADH
? + NAD+
2.9% activity compared to lipoamide
-
-
?
menadione + NADH
? + NAD+
2.9% activity compared to lipoamide
-
-
?
menadione + NADH
? + NAD+
-
13.6% of the activity with lipoamide
-
-
?
methylene blue + NADH
? + NAD+
-
9.4% of the activity with lipoamide
-
-
?
methylene blue + NADH + H
reduced methylene blue + NAD+
-
-
-
?
methylene blue + NADH + H
reduced methylene blue + NAD+
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
O2 + NADH
?
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
O2 + NADH
H2O2 + NAD+
-
40fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
-
-
?
O2 + NADH
H2O2 + NAD+
-
the enzyme produces reactive oxygen species, i.e. hydrogen peroxide, acting as an oxidase
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
233.4% activity compared to lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
233.4% activity compared to lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
12.3% of the activity with lipoamide
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
-
-
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
-
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
-
-
r
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes
-
-
r
thio-NAD+ + NADH
thio-NADH + NAD+
-
activity with wild-type enzyme and mutant enzymes C44S and C49S
-
-
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
-
-
?
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
-
-
-
additional information
?
-
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
-
additional information
?
-
the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the most important function of dehydrolipoamide dehydrogenase as a component of the pyruvate dehydrogenase and the 2-oxoglutarate dehydrogenase complex is the implication in the oxidative decarboxylation of pyruvate and 2-oxoglutarate
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is one of the major antigens for production of autoantibodies after infection with hepatitis C virus causing autoimmune phenomena like higher prevalences for liver cirrhosis, arthritis, abnormal liver function, and elevated alpha-FP levels, immunocolorimetrical determination of anti-E3 antibody titer after infection in several patients and of clinical manifestations, overview
-
-
-
additional information
?
-
-
DLD catalyzes the reduction of NAD+ by dihydrolipoamide and exhibits NADH-dependent diaphorase activity
-
-
-
additional information
?
-
-
DLD catalyzes the reduction of NAD+ by dihydrolipoamide and exhibits NADH-dependent diaphorase activity
-
-
-
additional information
?
-
enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosporylation, overview
-
-
-
additional information
?
-
-
the enzyme is required for hyperactivation, i.e. enhanced motility, and acrosome reaction of hamster spermatozoa, the post-pyruvate metabolic enzyme shows dual involvement and regulation during sperm capacitation, control of the directionality of enzyme activity during sperm capacitation
-
-
-
additional information
?
-
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
-
additional information
?
-
-
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
-
additional information
?
-
no activity with NADPH, potassium ferricyanide and methylene blue
-
-
-
additional information
?
-
-
reductive half-reaction, hydride transfer from NADH to FAD, is rate limiting when a quinone is the oxidant
-
-
-
additional information
?
-
-
EC 1.8.1.4 is the E3-protein component of the mitochondrial 2-oxoacid dehydrogenase multienzyme complexes and the L-protein component of the glycine decarboxylase system
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the physiological substrates are the dihydrolipoyl domain of the E2 component, dihydrolipoyl acyltransferase, of the 2-oxoacid dehydrogenase multienzyme complexs or the dihydrolipoyl H-protein of the mitochobdrial glycine decarboxylase
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
-
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
-
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
-
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
-
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
-
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
-
-
-
additional information
?
-
-
the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
-
-
-
additional information
?
-
-
the enzyme might play a role in modifying NO levels under specific cell conditions
-
-
-
additional information
?
-
-
LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
-
-
-
additional information
?
-
-
the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrated DNA + NAD(P)H
?
-
enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination which can cause cancer, enzyme might be resonsible for reversing biological nitration processes
-
-
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
-
enzyme reduces DNA nitro adducts including 8-nitroguanine, 3-nitrotyrosine, and 8-nitroxanthine, which formed in presence of peroxynitrite and nitryl chloride present in inflamed tissues, the nitrated DNA adducts are unstable and undergo spontaneous depurination
-
-
?
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
enzyme catalyzes the NAD+-dependent oxidation of dihydrolipoyl cofactors being covalently attached to the acyltransferase components of pyruvate dehydrogenase, 2-ketoglutarate dehydrogenase, and glycine reductase multienzyme complexes
-
-
r
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
reaction is important to protect the cell e.g. from oxidative stress
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
-
-
-
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
Q0KBV8
-
-
-
?
dihydrolipoamide + NAD
lipoamide + NADH + H+
-
-
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
A0A0H2Z9F5, A0A0H2ZB32, A0A0H2ZHZ0
-
-
-
r
dihydrolipoamide + NAD
lipoamide + NADH + H+
A0A0H2Z9F5, A0A0H2ZB32, A0A0H2ZHZ0
-
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
regulation of activity dependent on tyrosine-phosphorylation of the enzyme
-
-
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
the forward reaction is the physiological one
-
-
r
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
A0A0H2Z9F5, A0A0H2ZB32, A0A0H2ZHZ0
by cell lysate
-
-
?
phenazine-1-carboxylic acid + NADH + H
reduced phenazine-1-carboxylic acid + NAD+
A0A0H2Z9F5, A0A0H2ZB32, A0A0H2ZHZ0
by cell lysate
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protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
P0A9P0
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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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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+
A0A0K9R8G5
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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
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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 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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Q8NTE1
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
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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 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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Q811C4
enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosporylation, 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
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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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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
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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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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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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
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wild-type enzyme contains 1 FAD per subunit, mutant enzyme K37E has about 25% less bound FAD
FAD
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wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD
FAD
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tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
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the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates
FAD
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a flavoprotein, each monomer of 51000 Da binds one molecule of FAD
FAD
a single FAD is non-covalently arranged in each subunit
NAD+
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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+
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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+
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NAD+
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393971, 393993, 394003, 394004, 659101, 672869, 673943, 674382, 674759, 674943, 675350, 677161, 691569, 711099, 741807, 741998, 742087, 742221, 743051, 743127
NADH
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the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
N