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Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
for references in articles please use BRENDA:EC1.8.1.4
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.1 With NAD+ or NADP+ as acceptor
1.8.1.4 dihydrolipoyl dehydrogenase
IUBMB Comments
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 (click here 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 .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 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 Schemes
showSynonyms
lipoamide dehydrogenase, dihydrolipoamide dehydrogenase, dldh, dihydrolipoyl dehydrogenase, l-protein, nadh diaphorase, e3 component, lipdh, lipoyl dehydrogenase, nicotinamide adenine dinucleotide diaphorase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CIP50
coronin-interacting protein
dehydrogenase, lipoamide
-
-
-
-
dehydrolipoate dehydrogenase
-
-
-
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DHLDH
-
-
-
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DHLipDH
diaphorase
dihydrolipoamide dehydrogenase
dihydrolipoamide dehydrogenase E3
dihydrolipoamide:NAD+ oxidoreductase
dihydrolipoic dehydrogenase
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-
-
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dihydrolipoyl dehydrogenase
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-
-
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DLD
DLD1
Dld2
DLDH
DLDH2
E3
E3 component of 2-oxoglutarate dehydrogenase complex
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E3 component of acetoin cleaving system
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E3 component of alpha keto acid dehydrogenase complexes
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-
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E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
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E3 component of pyruvate complex
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-
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E3 lipoamide dehydrogenase
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EC 1.6.4.3
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formerly
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Glycine cleavage system L protein
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-
-
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Glycine oxidation system L-factor
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-
-
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LAD
LADH
LDH
LDP-Glc
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-
-
-
LDP-Val
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-
-
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LipDH
lipoamide dehydrogenase
lipoamide dehydrogenase (NADH)
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-
-
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lipoamide dehydrogenase C
lipoamide oxidoreductase (NADH)
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-
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lipoamide reductase
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-
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lipoamide-dehydrogenase-valine
lipoate dehydrogenase
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lipoic acid dehydrogenase
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lipoyl dehydrogenase
LPD
LPD-GLC
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-
-
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LPD-VAL
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-
-
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LPD1
LPD2
Lpd3
LpdA
LpdC
LpdG
LpdV
NAD(P)H:lipoamide oxidoreductase
NADH dehydrogenase
NADH diaphorase
NADH:lipoamide oxidoreductase
ORF-E3
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-
-
-
pdhL
rhDLDH
TAase
additional information
diaphorase
-
-
-
-
dihydrolipoamide dehydrogenase
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dihydrolipoamide dehydrogenase
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dihydrolipoamide dehydrogenase
Starkeyomyces koorchalomoides FDUS 0337
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-
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dihydrolipoamide dehydrogenase E3
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common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoamide dehydrogenase E3
-
common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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
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DLDH
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E3
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-
-
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E3
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-
E3
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E3
pyruvate dehydrogenase complex is composed of multiple copies of three catalytic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3)
LADH
Starkeyomyces koorchalomoides
-
LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity
LADH
Starkeyomyces koorchalomoides FDUS 0337
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LADH is an E3 component of pyruvate dehydrogenase complex with significant protein acetyltransferase activity
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lipoamide-dehydrogenase-valine
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is the specific E3 subunit for branched-chain keto acid dehydrogenase
lipoamide-dehydrogenase-valine
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is the specific E3 subunit for branched-chain keto acid dehydrogenase
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lipoyl dehydrogenase
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LPD
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-
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LPD1
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plastidial LPD1 encodes one of the two E3 isoforms found in the plastidial pyruvate dehydrogenase complex
NADH:lipoamide oxidoreductase
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-
-
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TAase
Starkeyomyces koorchalomoides
-
Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity
TAase
Starkeyomyces koorchalomoides FDUS 0337
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Starkeyomyces koorchalomoides transacetylase (TAase) is a dihydrolipoamide dehydrogenase and also exhibits diaphorase activity
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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
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
involvement of a reversibly reducible disulfide bond in catalytic mechanism
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping pong mechanism
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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+
Asp473 is important for efficient catalytic function of the enzyme
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
formation of a FADH2-NAD+ intermediate in catalysis, reaction mechanism of reductive and oxidative half-reactions involving enzyme, FAD/FADH2, and NAD+/NADH
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron-reduced enzyme, both redox centers are reduced, mechanism of the diaphorase reaction which occurs when the enzyme is in the four-electron-reduced state
-
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
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
A0A0K9R8G5
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
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
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
oxidation
-
catalyzes reoxidation of reduced lipoate attached to H-protein, a lipoic acid-containing protein
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
Biosynthesis of secondary metabolites, Citrate cycle (TCA cycle), Glycine, serine and threonine metabolism, Glycolysis / Gluconeogenesis, Lysine degradation, Microbial metabolism in diverse environments, Propanoate metabolism, Pyruvate metabolism, Tryptophan metabolism, Valine, leucine and isoleucine degradation
MetaCyc
2-oxoglutarate decarboxylation to succinyl-CoA, 2-oxoisovalerate decarboxylation to isobutanoyl-CoA, glycine biosynthesis II, glycine cleavage, pyruvate decarboxylation to acetyl CoA I
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,S)-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
r
1-methoxyphenazinium methosulfate + NADH
? + NAD+
Substrates: 248.1% activity compared to lipoamide
Products: -
Products: -
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
Substrates: cytochrome c is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
Products: -
Products: -
?
2-hydroxy-1,4-benzoquinone + NADH
2-hydroxy-1,4-benzoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
2-methyl-1,4-benzoquinone + NADH
2-methyl-1,4-benzoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
3-nitrotyrosine + NAD(P)H
3-aminotyrosine + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
3-nitrotyrosine + NADPH
3-aminotyrosine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
5-hydroxy-1,4-naphthoquinone + NADH
5-hydroxy-1,4-naphthoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
5-nitroblue tetrazolium chloride + NADH
? + NAD+
-
Substrates: 5.1% of the activity with lipoamide
Products: -
Products: -
?
8-nitroguanine + NAD(P)H
8-aminoguanine + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroguanine + NADPH
8-aminoguanine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroxanthine + NAD(P)H
8-aminoxanthine + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroxanthine + NADPH
8-aminoxanthine + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
benzyl viologen + NADH
? + NAD+
-
Substrates: 2.9% of the activity with lipoamide
Products: -
Products: -
?
dihydrolipoamide + NADP+
lipoamide + NADPH
-
Substrates: -
Products: -
Products: -
r
dihydrolipoate + NAD+
lipoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoic acid + NAD+
lipoic acid + NADH + H+
Substrates: -
Products: -
Products: -
?
DL-alpha-lipoamide + NADH
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
DL-lipoylpentanoate + NADH
? + NAD+
-
Substrates: 100fold reaction by the enzyme in two-electron-reduced state compared to the enzyme in four-electron-reduced state
Products: -
Products: -
?
ferrileghemoglobin + NADH + H+
ferroleghemoglobin + NAD+
Substrates: -
Products: -
Products: -
r
ferrocene + NADH
? + NAD+
Substrates: 3.6% activity compared to lipoamide
Products: -
Products: -
?
ferrocenecarboxylic acid + NADH
? + NAD+
Substrates: 4.1% activity compared to lipoamide
Products: -
Products: -
?
iodonitrotetrazolium chloride + NADH
? + NAD+
Substrates: 19.3% activity compared to lipoamide
Products: -
Products: -
?
lipoamide + 3-acetylpyridine adenine dinucleotide
dihydrolipoamide + ?
-
Substrates: -
Products: -
Products: -
?
lipoamide + nicotinamide hypoxanthine dinucleotide
dihydrolipoamide + ?
-
Substrates: -
Products: -
Products: -
?
lipoamide + thio-NADH
dihydrolipoamide + thio-NAD+
-
Substrates: -
Products: -
Products: -
?
lipoate + NADH + H+
dihydrolipoate + NAD+
-
Substrates: -
Products: -
Products: -
r
lipoyl H-protein + NADH + H+
dihydrolipoyl H-protein + NAD+
-
Substrates: -
Products: -
Products: -
r
metmyoglobin + NADH
reduced myoglobin + NAD+
-
Substrates: myoglobin is a poor electron acceptor, only in presence of methylene blue the enzyme shows some activity
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
nitrated DNA + NAD(P)H
?
-
Substrates: 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
Products: -
Products: -
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
-
Substrates: 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
Products: -
Products: -
?
nitrotetrazolium blue + NADH + H+
reduced nitrotetrazolium blue + NAD+
-
Substrates: -
Products: -
Products: -
r
oxidized lipoic acid + NADH
reduced lipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
?
protein N6-(dihydrolipoyl)lysine + NAD+
protein N6-(lipoyl)lysine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
reduced DL-lipoamide + NAD+
oxidized DL-lipoamide + NADH
-
Substrates: -
Products: -
Products: -
r
resazurin + NADH
? + NAD+
Substrates: 155.8% activity compared to lipoamide
Products: -
Products: -
?
resorufin + NADH
? + NAD+
Substrates: 19.1% activity compared to lipoamide
Products: -
Products: -
?
sulfonated tetrazolium WST-1 + NADH
formazan derivative + NAD+
Substrates: 39.2% activity compared to lipoamide
Products: -
Products: -
?
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
1,4-benzoquinone + NADH
1,4-benzoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: activity with wild-type enzyme and mutant enzymes C44S and C49S
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: -
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: -
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: -
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: 31.1% of the activity with lipoamide
Products: -
Products: -
?
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
Substrates: -
Products: -
Products: -
r
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
Substrates: -
Products: -
Products: -
r
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
Substrates: -
Products: -
Products: -
r
2,6-dimethoxy-1,4-benzoquinone + NADH
? + NAD+
Substrates: 8.0% activity compared to lipoamide
Products: -
Products: -
?
2,6-dimethoxy-1,4-benzoquinone + NADH
? + NAD+
Substrates: 8.0% activity compared to lipoamide
Products: -
Products: -
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
2,6-dimethyl-1,4-benzoquinone + NADH
2,6-dimethyl-1,4-benzoquinol + NAD+
-
Substrates: 90fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
Products: -
Products: -
?
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
Substrates: -
Products: -
Products: -
?
2-(p-iodophenyl)-3-p-nitrophenyl-5-phenyltetrazolium chloride + NADH
? + NAD+
Substrates: -
Products: -
Products: -
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
-
Substrates: -
Products: -
Products: -
?
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide + NADH
?
-
Substrates: -
Products: -
Products: -
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
-
Substrates: -
Products: -
Products: -
?
3-nitrotyrosine + dihydrolipoic acid
3-aminotyrosine + lipoic acid + H2O
-
Substrates: -
Products: -
Products: -
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
-
Substrates: -
Products: -
Products: -
?
3-nitrotyrosine + ubiquinol
3-aminotyrosine + ubiquinone + H2O
-
Substrates: -
Products: -
Products: -
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroguanine + dihydrolipoic acid
8-aminoguanine + lipoic acid + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroguanine + ubiquinol
8-aminoguanine + ubiquinone + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroxanthine + dihydrolipoic acid
8-aminoxanthine + lipoic acid + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
-
Substrates: -
Products: -
Products: -
?
8-nitroxanthine + ubiquinol
8-aminoxanthine + ubiquinone + H2O
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
Starkeyomyces koorchalomoides
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH
dihydrolipoamide + NAD+
Starkeyomyces koorchalomoides FDUS 0337
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
Substrates: -
Products: -
Products: -
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
Substrates: -
Products: -
Products: -
?
alpha-lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: DLDH activity, forward reaction
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
Azotobacter agilis
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: mutant enzymes C44S and C49S show minute activity
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Escherichia coli B / ATCC 11303
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: regulation of activity dependent on tyrosine-phosphorylation of the enzyme
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: the forward reaction is the physiological one
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: alternate oxidation and reduction of an intrachain disulfide bond
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Leishmania donovani BHU1081
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
A0A0K9R8G5
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
Substrates: specific substrate
Products: -
Products: -
?
DL-lipoamide + NADH
DL-dihydrolipoamide + NAD+
-
Substrates: specific substrate
Products: -
Products: -
?
DL-lipoamide + NADH + H+
DL-dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
DL-lipoamide + NADH + H+
DL-dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
lipoamide + NADH
dihydrolipoamide + NAD+
Substrates: NADH:lipoamide oxidoreductase activity, reverse reaction
Products: -
Products: -
r
lipoamide + NADH
dihydrolipoamide + NAD+
Substrates: -
Products: -
Products: -
r
lipoamide + NADH
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
lipoamide + NADH
dihydrolipoamide + NAD+
Substrates: 100% activity
Products: -
Products: -
?
lipoamide + NADH
dihydrolipoamide + NAD+
Substrates: 100% activity
Products: -
Products: -
?
lipoamide + NADH
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
r
lipoamide + NADH + H+
dihydrolipoamide + NAD+
Substrates: -
Products: -
Products: -
?
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
r
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
r
lipoic acid + NADH
dihydrolipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
?
lipoic acid + NADH
dihydrolipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
?
lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
r
lipoic acid + NADH + H+
dihydrolipoic acid + NAD+
-
Substrates: -
Products: -
Products: -
r
mature frataxin + NADH
denoted frataxin + NAD+
-
Substrates: cleavage by C-term DLD
Products: -
Products: -
?
mature frataxin + NADH
denoted frataxin + NAD+
-
Substrates: cleavage by C-term DLD
Products: -
Products: -
?
mature frataxin + NADH
denoted frataxin + NAD+
-
Substrates: exhibits DLD activity but is proteolytically inactive against mature frataxin. Purified pig DLD preparation exhibits weak but clear proteolytic activity
Products: -
Products: -
?
menadione + NADH
? + NAD+
Substrates: 2.9% activity compared to lipoamide
Products: -
Products: -
?
menadione + NADH
? + NAD+
Substrates: 2.9% activity compared to lipoamide
Products: -
Products: -
?
menadione + NADH
? + NAD+
-
Substrates: 13.6% of the activity with lipoamide
Products: -
Products: -
?
methylene blue + NADH
? + NAD+
-
Substrates: 9.4% of the activity with lipoamide
Products: -
Products: -
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
Substrates: -
Products: -
Products: -
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
Substrates: -
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
naphthoquinone + NADH
1,4-naphthoquinol + NAD+
-
Substrates: -
Products: -
Products: -
?
nitro blue tetrazolium + NADH
? + NAD+
Substrates: -
Products: -
Products: -
?
nitro blue tetrazolium + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
nitrotetrazolium blue + NADH
? + NAD+
Substrates: 2.9% activity compared to lipoamide
Products: -
Products: -
?
nitrotetrazolium blue + NADH
? + NAD+
Substrates: 2.9% activity compared to lipoamide
Products: -
Products: -
?
O2 + NADH
?
-
Substrates: activity with wild-type enzyme and mutant enzymes C44S and C49S
Products: -
Products: -
?
O2 + NADH
H2O2 + NAD+
-
Substrates: 40fold reaction by the enzyme in four-electron-reduced state compared to the enzyme in two-electron-reduced state
Products: -
Products: -
?
O2 + NADH
H2O2 + NAD+
-
Substrates: the enzyme produces reactive oxygen species, i.e. hydrogen peroxide, acting as an oxidase
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: activity with wild-type enzyme and mutant enzymes C44S and C49S
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
Substrates: 233.4% activity compared to lipoamide
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
Substrates: 233.4% activity compared to lipoamide
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
Substrates: 12.3% of the activity with lipoamide
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: by cell lysate
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: 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
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: by cell lysate
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: 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
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
Products: -
Products: -
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
A0A0K9R8G5
Substrates: -
Products: -
Products: -
r
pyocyanin + NADH + H+
reduced pyocyanin + NAD+
Substrates: pyocyanin is reported to stimulate respiration
Products: -
Products: -
?
pyocyanin + NADH + H+
reduced pyocyanin + NAD+
Substrates: pyocyanin is reported to stimulate respiration
Products: -
Products: -
?
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
Substrates: 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
Products: -
Products: -
r
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
Substrates: -
Products: -
Products: -
r
thio-NAD+ + NADH
thio-NADH + NAD+
-
Substrates: activity with wild-type enzyme and mutant enzymes C44S and C49S
Products: -
Products: -
?
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
Substrates: enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
Products: -
Products: -
?
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
Substrates: reaction is important to protect the cell e.g. from oxidative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADH:NAD+ transhydrogenase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the reoxidation of the covalently bound reduced lipoic acid cofactor of the E2 subunits of all the mitochondrial alpha-keto acid dehydrogenase multienzyme complexes including the alpha-ketoglutarate dehydrogenase complex, the pyruvate dehydrogenase complex, and the branched-chain alpha-keto acid dehydrogenase complex
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also shows diaphorase activity with 2,6-dichlorophenol indophenol and thiazolyl blue tetrazolium bromide
Products: -
Products: -
?
additional information
?
-
Leishmania donovani BHU1081
-
Substrates: the enzyme also shows diaphorase activity with 2,6-dichlorophenol indophenol and thiazolyl blue tetrazolium bromide
Products: -
Products: -
?
additional information
?
-
-
Substrates: DLD catalyzes the reduction of NAD+ by dihydrolipoamide and exhibits NADH-dependent diaphorase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: DLD catalyzes the reduction of NAD+ by dihydrolipoamide and exhibits NADH-dependent diaphorase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: diaphorase activity
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosphorylation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with NADPH, potassium ferricyanide and methylene blue
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NADPH, potassium ferricyanide and methylene blue
Products: -
Products: -
?
additional information
?
-
-
Substrates: reductive half-reaction, hydride transfer from NADH to FAD, is rate limiting when a quinone is the oxidant
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme lacks diaphorase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme might play a role in modifying NO levels under specific cell conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: LAD is unable to convert formamidoxim, acetone oxime, acetohydroxamic acid, and Nomega-hydroxy-L-arginine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
r
nitrated DNA + NAD(P)H
?
-
Substrates: 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
Products: -
Products: -
?
nitrated DNA + NADPH
DNA + NADP+ + H2O
-
Substrates: 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
Products: -
Products: -
?
protein N6-(dihydrolipoyl)lysine + NAD+
protein N6-(lipoyl)lysine + NADH + H+
-
Substrates: -
Products: -
Products: -
?
reduced lipoamide + NAD+
oxidized lipoamide + NADH
-
Substrates: 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
Products: -
Products: -
r
ubiquinone-10 + NAD(P)H
ubiquinol-10 + NAD(P)+
-
Substrates: reaction is important to protect the cell e.g. from oxidative stress
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
-
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
Substrates: -
Products: -
Products: -
?
alpha-lipoamide + NADH + H+
dihydrolipoamide + NAD+
Substrates: -
Products: -
Products: -
?
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: regulation of activity dependent on tyrosine-phosphorylation of the enzyme
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH
-
Substrates: the forward reaction is the physiological one
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
-
Substrates: -
Products: -
Products: -
r
dihydrolipoamide + NAD+
lipoamide + NADH + H+
A0A0K9R8G5
Substrates: -
Products: -
Products: -
r
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: by cell lysate
Products: -
Products: -
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
Substrates: by cell lysate
Products: -
Products: -
?
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
-
Substrates: -
Products: -
Products: -
r
protein N6-(lipoyl)lysine + NADH + H+
protein N6-(dihydrolipoyl)lysine + NAD+
A0A0K9R8G5
Substrates: -
Products: -
Products: -
r
ubiquinone + NAD(P)H
ubiquinol + NAD(P)+
-
Substrates: enzyme is involved in extramitochondrial regeneration of the important antioxidant ubiquinol required for cell protection against peroxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an essential component of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is involved in capacitation of spermatozoa in hamster, enzyme regulation in spermatozoa via tyrosine-phosphorylation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: LPD-Val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase, LPD-Glc fulfills all other requirements for lipoamide dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: lack of dihydrolipoamide dehydrogenase results in a deficiency in alpha-galactoside metabolism and galactose transport
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme might play a role in modifying NO levels under specific cell conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme fulfills its function in the pyruvate, 2-oxoglutarate and branched-chain 2-oxoacid dehydrogenase complexes and in the glycine cleavage system
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD
FAD
-
the fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature
FAD
-
wild-type enzyme contains 1 FAD per subunit, mutant enzyme K37E has about 25% less bound FAD
FAD
-
tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
-
the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates
FAD
-
tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
-
a flavoprotein, each monomer of 51000 Da binds one molecule of FAD
FAD
a single FAD is non-covalently arranged in each subunit
FAD
one FAD as a prosthetic group at each subunit, binding structure analysis
NAD+
-
-
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+
-
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
NADH
-
the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
additional information
-
enzyme contains a redox-active disulfide, the cofactor cycles between reduced and oxidized state during catalysis
-
additional information
-
enzyme contains a redox-active disulfid, the cofactor cycles between reduced and oxidized state during catalysis, in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron.reduced enzyme, both redox centers are reduced
-
additional information
FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
-
additional information
-
FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
-
additional information
-
contains neither FMN nor FAD in the molecule
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM
Fe
-
amino acid sequence homology indicates the presence of a Fe-containing rubredoxin-like domain. The amount of iron is determined to be 1.1 molecule per rDiaA molecule by ICP atomic emission spectroscopy
Mg2+
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
Zn2+
additional information
Zn2+
-
highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM, Zn2+ slightly elevates the pH-optimum of the enzyme
additional information
1 mM Na+, Ca2+, Mg2+, Mn2+, Fe3+, Zn2+, Pb2+, and Hg2+ do not enhance enzyme activity
additional information
-
1 mM Na+, Ca2+, Mg2+, Mn2+, Fe3+, Zn2+, Pb2+, and Hg2+ do not enhance enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-bis(2-chloroethyl)-1-nitrourea
-
after reduction of the oxidized form of enzyme to the two-electron-reduced state
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
at higher concentrations (2 mM) significantly inhibits the lipoamide dehydrogenase activity
1-methyl-4-phenylpyridinium
-
at lower concentrations (1 mM) as compared to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine significantly inhibits the lipoamide dehydrogenase activity
10-(2-dimethylaminopropyl)-dibenzothiazine cation radical
-
60% inactivation after 10 min incubation and 79% after 30 min using the myeloperoxidase system, 72% inactivation after 10 min incubation using the horseradish peroxidase system
10-(2-methyl,3-dimethylaminopropyl)-dibenzothiazine cation radical
-
90% inactivation after 10 min and 30 min incubation using the myeloperoxidase system, 94% inactivation after 10 min incubation using the horseradish peroxidase system
10-(3-dimethylaminopropyl)-dibenzothiazine cation radical
-
87% inactivation after 10 min incubation and 89% after 30 min using the myeloperoxidase system, 94% inactivation after 10 min incubation using the horseradish peroxidase system
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine hydrochloride
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-amino-4-hydroxy-6-methyl-7,8-dihydropteridine
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
2-chloro-10-(3-dimethylaminopropyl)-dibenzothiazine cation radical
-
45% inactivation after 10 min incubation and 75% after 30 min using the myeloperoxidase system, 89% inactivation after 10 min incubation using the horseradish peroxidase system
2-chloro-10-[3-(1-methyl-4-piperazinyl)-propyl]-dibenzothiazine cation radical
-
54% inactivation after 10 min incubation and 80% after 30 min using the myeloperoxidase system, 90% inactivation after 10 min incubation using the horseradish peroxidase system
2-chloro-10-[3-[1-(2-hydroxyethyl)-4-piperazinyl]propyl]-dibenzothiazine cation radical
-
42% inactivation after 10 min incubation and 69% after 30 min using the myeloperoxidase system, 79% inactivation after 10 min incubation using the horseradish peroxidase system
2-methylmercapto-10-[2-(1-methyl-2-piperidinyl)-ethyl]-dibenzothiazine cation radical
-
77% inactivation after 10 min incubation and 82% after 30 min using the myeloperoxidase system, 85% inactivation after 10 min incubation using the horseradish peroxidase system
2-propionyl-10-(3-dimethylaminopropyl)-dibenzothiazine cation radical
-
11% inactivation after 10 min incubation and 32% after 30 min using the myeloperoxidase system, 83% inactivation after 10 min incubation using the horseradish peroxidase system
2-trifluoromethyl-10-[3-(1-methyl-4-piperazinyl)propyl]-dibenzothiazine cation radical
-
5% inactivation after 10 min incubation and 16% after 30 min using the myeloperoxidase system, 67% inactivation after 10 min incubation using the horseradish peroxidase system
2-trifluoromethyl-10-[3-(dimethylamino)propyl]-dibenzothiazine cation radical
-
2% inactivation after 10 and 30 min incubation using the myeloperoxidase system, 16% inactivation after 10 min incubation using the horseradish peroxidase system
2-trifluoromethyl-10-[3-[1-(2-hydroxyethyl)4-piperazinyl]propyl]-dibenzothiazine cation radical
-
1% inactivation after 10 min incubation and 8% after 30 min using the myeloperoxidase system, 61% inactivation after 10 min incubation using the horseradish peroxidase system
2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]-N-[3-(trifluoromethyl)benzyl]acetamide
-
Cd2+
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
chlorpromazine
-
0.1 mM, 75% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 94% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 89% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
cyanide
slight inhibition; slight inhibition; slight inhibition
Diethylamine NONOate
-
induces 71% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
diphenyleneiodonium
an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro; an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro; an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro
Fe2+
-
at high concentrations has significant inhibitory effect on the lipoamide dehydrogenase activity
fluphenazine
-
0.1 mM, 53% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 61% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
folic acid
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
Guanidine-HCl
-
4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible
H2O2
-
enzyme is inactivated by complex III- but not complex I-derived reactive oxygen species, and the accompanying loss of activity due to the inactivation can be restored by cysteine and glutathione. H2O2 instead of superoxide anion is responsible for the inactivation, and protein sulfenic acid formation is associated with the loss of enzymatic activity
Hg2+
1 mM shows strong inhibitory effect on recombinant rBfmBC activity (more than 80% inhibition)
isobiopterin
-
inhibition of NADH-lipoamide oxidoreductase activity, no effect on diaphorase activity and transhydrogenase activity
N-[2-(2,4-dichlorophenyl)ethyl]-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]acetamide
most potent inhibitor, noncompetitive versus NADH, NAD+, and lipoamide
p-[(bromoacetyl)-amino]phenyl arsenoxide
-
irreversible active site directed inactivation
Pb2+
1 mM shows strong inhibitory effect on recombinant BfmBC activity (more than 80% inhibition)
perphenazine
-
0.1 mM, 69% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 75% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 79% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
phenothiazine cation radicals
-
irreversible inactivation dependent on time, radical structure, and radical production enzyme system, radicals are produced by reaction of myeloperoxidase or horse radish peroxidase on the phenothiazines promazine, trimeprazine, thioridazine, chlorpromazine, prochlorperazine, promethazine, and others, in presence of H2O2, protection by radical scavengers e.g. thiol compounds, amino acids and peptides, pyridine dinucleotides like NADH, or best by ascorbate and trolox, overview
potassium phosphate
-
when purified DLDH is eluted directly into potassium phosphate buffer, the enzymatic activity rapidly decreases
prochlorperazine
-
0.1 mM, 80% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 85% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 80% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
promazine
-
0.1 mM, 89% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 93% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 94% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4, 94% inhibition in the presence of 0.2 mM NADH, 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 after 10 min incubation
Promethazine
-
0.1 mM, 79% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 51% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 72% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
propericyazine
-
0.1 mM, 40% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4
propionylpromazine
-
0.1 mM, 32% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 88% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 83% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
S-nitrosocysteine
-
induces a 62% loss in diaphorase activity at 2 mM and an 88% loss at 10 mM
S-nitrosoglutathione
-
induces 84% loss in diaphorase activity at 10 mM, but does not induce any activity loss at 2 mM
thioridazine
-
0.1 mM, 82% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 97% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 85% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4, 85% inhibition in the presence of 0.1 mM NADH, 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 after 10 min incubation
Trifluoperazine
-
0.1 mM, 16% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 72% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 67% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
triflupromazine
-
0.1 mM, 68% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 16% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
trimeprazine
-
0.1 mM, 90% inactivation, in the presence of 0.5 U/ml myeloperoxidase and 0.1 mM H2O2 at pH 7.4, 90% inactivation, in the presence of 0.005 mM myoglobin and 0.25 mM H2O2 at pH 7.4, 94% inactivation in the presence of 0.5 U/ml horseradish peroxidase and 0.2 mM H2O2 at pH 7.4
valproyl-dephosphoCoA
-
uncompetitive inhibitor, 0.5-1.0 mM inhibit DLDH activity
5-methoxyindole-2-carboxylic acid
specific inhibitor, inhibition in vivo blocks acrosome reaction completely and hyperactivation partially
5-methoxyindole-2-carboxylic acid
-
specific inhibitor of DLD, dibutryl cyclic adenosine monophosphate and the calcium ionophore A23187 can significantly reverse the inhibitory effect on sperm acrosome reaction
arsenite
activity of lipoamide dehydrogenase in isolated mitochondria is sensitive to arsenite, but not arsenate
arsenite
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
arsenite
-
reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity
NAD+
-
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
NADH
strong substrate inhibition at concentrations higher than 0.015 mM
NADH
-
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
p-Aminophenyldichloroarsine
-
inactivated only in presence of NADH and dihydrolipoamide, no significant loss of activity in absence of NADH and dihydrolipoamide
Zn2+
about 30% inhibition of recombinant BfmBC activity with 5 mM
additional information
-
LAD is not inhibited by resorufin ethyl ether, phenidone, Nomega-nitro-L-arginine methyl ester hydrochloride, proadiphen hydrochloride, and miconazole nitrate
-
additional information
-
expression of LRG-47, as well as IFNgamma stimulation, block intracellular interaction of coronin-1 with LpdC
-
additional information
-
expression of LRG-47, as well as IFNgamma stimulation, block intracellular interaction of coronin-1 with LpdC
-
additional information
-
diamide, GSH, GSSG, cysteine and nitrite do not exhibit any inhibitory effects
-
additional information
-
no age-related decline in DLDH activity or expression is evident in rats over the period from 5 to 30 months of age. Lower DLDH dehydrogenase activity observed in pups may be due to NADH inhibition
-
additional information
-
no inhibition of the nitric oxide reduction by cyanide, antimycin A, or diphenyleneiodonium ions
-
additional information
-
LAD is not inhibited by resorufin ethyl ether, phenidone, Nomega-nitro-L-arginine methyl ester hydrochloride, proadiphen hydrochloride, and miconazole nitrate
-
additional information
-
no inhibition by the cation radical of 2-cyano-10-[3-(4-hydroxypiperidinyl)propyl]-dibenzothiazine in either peroxidase system
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
EDTA
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
lipoic acid
-
increase in activity might be due to formation of dihydrolipoic acid in the assay system
NAD+
0.2 mM NAD+ demonstrates a strong activating effect on LPD, and the activity is 5.2 times higher than that without NAD+
ubiquinone
-
slight increase in activity might be due to formation of ubiquinol in the assay system
additional information
-
activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation. Freezing-thawing results in further activation
-
additional information
-
activity of DLDH diaphorase is both protein amount- and time-dependent
-
additional information
-
activity of DLDH dehydrogenase increases in rats between 10 and 20 days of age. Dehydrogenase activity of DLDH shows a further, progressive increase in rats from 20 days to adulthood, in the absence of any further change in DLDH expression or diaphorase activity
-
additional information
-
activation of DLD proteolytic activity by high salt concentrations during hydroxyapatite fractionation, Freezingthawing results in further activation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.63
alpha-lipoamide
Starkeyomyces koorchalomoides
-
in 0.1 mM Tris-HCl (pH 7.0), 0.0005 mM EDTA, 0.01 mM beta2-mercaptoethanol, at 37°C
0.46
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.45
2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.0157
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI
0.0177
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI
0.0243
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.0274
dihydrolipoamide
pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI
0.0364
dihydrolipoamide
pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI
0.04
dihydrolipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain
0.064
dihydrolipoamide
-
recombinant DLDH expressed without lipoic acid
0.64
dihydrolipoamide
wild type enzyme, at pH 8.0 and 37°C
15.83
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
17.18
formaldoxime
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.27
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
16.93
glycerol trinitrate
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.56
Lipoamide
-
reaction with 3-acetylpyridine adenine dinucleotide
3.3
Lipoamide
in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
6.4
Lipoamide
-
reaction with nicotinamide hypoxanthine dinucleotide
0.182
NAD+
pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI
0.186
NAD+
pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI
0.288
NAD+
pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI
0.292
NAD+
pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI
0.312
NAD+
pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI
0.82
NAD+
-
recombinant DLDH expressed without without a lipoyl protein domain
0.0061
NADH
in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
5.48
S-nitroso-N-acetylpenicillamine
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.44
S-nitrosoglutathione
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.26
sodium nitroprusside
-
in the presence of superoxide dismutase, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
additional information
additional information
-
dehydrogenase and oxidase activity 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 4°C and 25°C, respectively
-
additional information
additional information
A0A0K9R8G5
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
kinetic analysis and modelling, detailed overview
-
additional information
additional information
kinetic analysis and mechanisms of wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michaelis?Menten kinetics
-
additional information
additional information
Michaelis?Menten kinetics
-
additional information
additional information
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
kinetic analysis and modelling, detailed overview
-
additional information
additional information
kinetic analysis and modelling, detailed overview
-
additional information
additional information
-
kinetic analysis and modelling, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
448
dihydrolipoamide
-
pH 8.0, 25°C, mitochondrial isozyme, reverse reaction, varying conditions
899
dihydrolipoamide
wild type enzyme, at pH 8.0 and 37°C
135.5 - 337
Lipoamide
-
pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions
135.5 - 337
NAD+
-
pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions
506
NAD+
-
recombinant DLDH expressed without without a lipoyl protein domain
448
NADH
-
pH 8.0, 25°C, mitochondrial isozyme, reverse reaction, varying conditions
additional information
additional information
-
turnover numbers for small polypeptides derived from proteolytic treatment of the H-protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000865
N-[2-(2,4-dichlorophenyl)ethyl]-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]acetamide
pH and temperature not specified in the publication
additional information
additional information
-
Zn2+ inhibition kinetics and mechanism
-
0.29
diphenyleneiodonium chloride
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.31
diphenyleneiodonium chloride
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.35
diphenyleneiodonium chloride
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.45
diphenyleneiodonium chloride
-
using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.56
diphenyleneiodonium chloride
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.6
diphenyleneiodonium chloride
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.8
diphenyleneiodonium chloride
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.0488
Lipoamide
-
recombinant DLDH expressed without lipoic acid, in the presence of 4 mM NAD+
0.1899
Lipoamide
-
recombinant DLDH expressed without lipoic acid, in the presence of 1.5 mM dihydrolipoamide
0.1953
Lipoamide
-
recombinant DLDH, in the presence of 1.5 mM dihydrolipoamide
0.349
Lipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 4 mM NAD+
0.8793
Lipoamide
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide
0.0044
NADH
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide
0.0107
NADH
-
recombinant DLDH expressed without lipoic acid, in the presence of 1.5 mM dihydrolipoamide
0.0149
NADH
-
recombinant DLDH, in the presence of 1.5 mM dihydrolipoamide
0.0351
NADH
-
recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 2 mM NAD+
0.084
NADH
-
recombinant DLDH expressed without lipoic acid, in the presence of 2 mM NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]-N-[3-(trifluoromethyl)benzyl]acetamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0009
N-[2-(2,4-dichlorophenyl)ethyl]-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl]acetamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.59
diphenyleneiodonium chloride
Sus scrofa
-
using hydroxylamine hydrochloride as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
0.68
diphenyleneiodonium chloride
Sus scrofa
-
using sodium nitroprusside as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.75
diphenyleneiodonium chloride
Sus scrofa
-
using S-nitroso-N-acetylpenicillamine as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.81
diphenyleneiodonium chloride
Sus scrofa
-
using S-nitrosoglutathione as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
1.93
diphenyleneiodonium chloride
Sus scrofa
-
using glycerol trinitrate as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
2.61
diphenyleneiodonium chloride
Sus scrofa
-
using formaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
3.31
diphenyleneiodonium chloride
Sus scrofa
-
using acetaldoxime as substrate, in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.19
-
substrate 5,5'-dithiobis-(2-nitrobenzoic acid), 30°C, pH 6.5
16.2
pH 7.0, 30°C, mutant enzyme E423D, assay in the presence of 2 M KCI
19.1
pH 7.0, 30°C, wild-type enzyme, assay in the presence of 2 M KCI
2.5
crude extract, in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
20
5.8
pH 7.0, 30°C, mutant enzyme E423S, assay in the presence of 2 M KCI
59.2
after 23.9fold purification, in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C
6.2
pH 7.0, 30°C, mutant enzyme E423A, assay in the presence of 2 M KCI
6.4
6.65
19.3fold purified enzyme, in 50 mM potassium phosphate buffer, pH 6.7, at 37°C
additional information
6.4
pH 7.0, 30°C, mutant enzyme E423Q, assay in the presence of 2 M KCI
additional information
-
mutant P453V shows a specific activity of 0.37 units/mg at the saturated substrate concentrations of 2 mM dihydrolipoamide and 3 mM NAD+ at 37°C in a 50 mM potassium phosphate buffer (pH 8.0) containing 1.5 mM EDTA
additional information
wild type enzyme: 586.50 units/mg protein, mutant N286D: 179.65 units/mg protein, mutant N286Q: 143.15 units/mg protein, mutant D320N: 283.10 units/mg protein
additional information
-
wild type enzyme: 586.50 units/mg protein, mutant N286D: 179.65 units/mg protein, mutant N286Q: 143.15 units/mg protein, mutant D320N: 283.10 units/mg protein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
reduction of nitric oxide, lioamide, lipoic acid, and 2,6-dichlorophenolindophenol
7 - 7.5
7.4
7.5
8.5
additional information
8.5
wild-type enzyme and mutant enzymes E423D, E423Q, E423S, and E423A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH 5.0: about 10% of maximal activity, pH 7.0-7.5: 60-70% of maximal activity, pH 8.0-8.5: 90% of maximal activity, pH 10.0: 10% of maximal activity in carbonate buffer
5.5 - 7.5
-
pH 5.5: about 75% of maximal activity, pH 7.5: about 40% of maximal activity, NADH-lipoamide oxidoreductase activity
6.5 - 8.5
-
pH 6.5: about 40% of maximal activity, pH 8.5: about 50% of maximal activity
7.5 - 8.8
-
pH 7.5: about 50% of maximal activity, pH 8.8: about 60% of maximal activity, dihydrolipoamide-NAD+ oxidoreductase activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
40
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diyhdrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex
-
-
brenda
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
3D7, 2 lipdh genes encoding 2 isozymes in mitochondrion and apicoplast, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
immunochemical analysis of dihydrolipoamide dehydrogenase protein levels
brenda
-
enzyme is not detected on Western blots probed with antibodies that recognize mitochondrial dihydrolipoamide dehydrogenase
brenda
additional information
-
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)
brenda
-
significant increase in DLDH dehydrogenase activity in rats only for the period between 30 and 60 days of age
brenda
-
significant increase in DLDH dehydrogenase activity in rats only for the period between 30 and 60 days of age
brenda
-
increase in DLDH dehydrogenase activity in rats between 10 and 20 days of age, with no further increase evident thereafter
brenda
additional information
mtLPD2 has a tissue-dependent expression pattern
brenda
additional information
-
mtLPD2 has a tissue-dependent expression pattern
brenda
additional information
-
both genes are transcribed during erythrocytic development of the parasite
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to the matrix, release of enzyme during acrosomal exocytosis
-
brenda
-
juxtanuclear localization, like Golgi, in spermatids
brenda
additional information
-
in the human malaria parasite Plasmodium falciparum, the single PDC enzyme complex with enzyme E3 is located exclusively in the apicoplast
brenda
-
Lpd1 protein is localized in the mitochondria during the logarithmic yeast growth and the filamentous growth
brenda
-
Lpd1 protein is localized in the mitochondria during the logarithmic yeast growth and the filamentous growth
-
brenda
E3 is a mitochondrial protein that is synthesized in precursor form in the cytoplasm. The precursor E3 for humans has a leader sequence composed of 35-amino acids at its amino-terminus, which is cleaved off during its import into the mitochondria matrix
brenda
-
isozyme mLipDH is a component of the branched-chain 2-ketoacid dehydrogenase and the 2-ketoglutarate dehydrogenase multienzyme complexes
brenda
-
enzyme is part of multienzyme complexes in the inner mitochondrial membrane
brenda
additional information
-
release of enzyme during acrosomal exocytosis, extramitochondrial localization in epididymal spermatozoa in mammalia
-
brenda
additional information
-
subcellular localization study using recombinant expression of the isozymes fused to fluorescent protein tags
-
brenda
additional information
-
synthesized predominantly on free ribosomes and translocated into mitochondria
-
brenda
additional information
-
no DLDH diaphorase activity in the cytosol
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
A0A0K9R8G5
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
E3 belongs to the pyridine nucleotide-disulfide oxidoreductase family along with glutathione reductase (GR), thioredoxin reductase, mercuric reductase and trypanothione reductase
evolution
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
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
evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
evolution
dihydrolipoamide dehydrogenase is a member of the disulfide oxidoreductase family
malfunction
-
the homozygous deletion mutant lpd1/lpd1 is unable to grow on non-fermentable carbon sources including glycerol, ethanol, acetate, and citrate. In addition, the lpd1/lpd1 strain exhibits a slow-growth phenotype on glucose-containing media and a marked sensitivity to 0.5 mM of hydrogen peroxide and shows filamentation defects
malfunction
-
enhanced arsenate and arsenite sensitivity is due to the disruption of the plastidial LPD1 and LPD2 genes
malfunction
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
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
-
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
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
-
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
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
chronic inhibition of the enzyme can attenuate oxidative stress in type 2 diabetes
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
-
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
metabolism
A0A0K9R8G5
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
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
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
physiological function
-
effects of insulin treatment on HuC/HuD myoenteric neurons, NADH diaphorase, and nNOS-positive myoenteric neurons of the duodenum of adult rats with acute diabetes is investigated: The density of NADH diaphorase-positive neurons in animals from the diabetic group and in the insulin treated diabetic group is greater than in the control group, indicating that short-term diabetes increases the activity of respiratory chain enzymes
physiological function
Starkeyomyces koorchalomoides
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
physiological function
-
dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of pyruvate dehydrogenase complex. LPD1 is required for filamentous growth under a serum-containing hyphal-inducing condition
physiological function
LPD is a useful biocatalyst for regenerating NAD+
physiological function
-
plastidial LPD expression quantitatively controls Arabidopsis arsenate sensitivity
physiological function
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
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
-
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
-
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
A0A0K9R8G5
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
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
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
human dihydrolipoamide dehydrogenase is a flavoenzyme component (E3) of the human 2-oxoglutarate dehydrogenase complex and few other dehydrogenase complexes
physiological function
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
-
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
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
-
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
-
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
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
-
dihydrolipoamide dehydrogenase is a component in the pyruvate-, 2-oxooglutarate- and branched-chain oxoacid dehydrogenase complexes and in the glycine cleavage system
physiological function
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
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
-
the enzyme regulates cystine deprivation-induced ferroptosis in head and neck cancer
physiological function
-
the enzyme is involved in adhesion to polystyrene as well as coelomocytes and other tissues like body wall, tentacle, muscle, respiratory tree and intestine from sea cucumber Apostichopus japonicas
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
Starkeyomyces koorchalomoides FDUS 0337
-
the protein acetyltransferase activity of LADH can be attributed as a moonlighting function of the enzyme
-
physiological function
-
LPD is a useful biocatalyst for regenerating NAD+
-
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
-
the enzyme is involved in adhesion to polystyrene as well as coelomocytes and other tissues like body wall, tentacle, muscle, respiratory tree and intestine from sea cucumber Apostichopus japonicas
-
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
-
physiological function
-
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
-
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. 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. 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. 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
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
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
additional information
conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity
additional information
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
-
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
location of residues Pro156 and Pro303 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
location of residue Cys50 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
location of residue H329 in human E3 enzyme, structure comparisons with E3 enzymes from other species
additional information
-
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
-
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
-
mitochondrial lipoamide dehydrogenase is an important protein for determining the sensitivity of oxidative metabolism to arsenate in Arabidopsis thaliana
additional information
-
molecular dynamics simulation the conformation of enzyme LADH that is proposed to be compatible with the reactive oxygen species (ROS) generation
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. 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
-
additional information
-
structure homology modeling of rhDLDH using the crystal structure of Mycobacterium tuberculosis DLDH, PDB 2A8X, chain A, as template
-
Show AA Sequence and Transmembrane Helices (34751 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102000
105000
110000
112000
115000
119000
28000
-
recombinant protein using SDS-PAGE, in good agreement with the calculated molecular weight of recombinant DiaA
50000
50027
x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis
51000
52000
52614
-
x * 52614, enzyme from chloroplast, electrospray mass spectrometry
53000
54000
55000
56000
57200
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
58000
75600
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis
dimer
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration
additional information
-
in solution LpD exists as an equilibrium mixture of a dimer and a tetramer, small-angle X-ray scattering and analytical ultracentrifugation
additional information
-
the homodimeric enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex
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 the E3 component of 2-keto acid dehydrogenase multienzyme complex
additional information
-
the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions
additional information
-
2 distinct dihydrolipoamide dehydrogenases, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
additional information
-
E3 enzyme homology structure modelling using the human enzyme structure, PDB ID 2F5Z
additional information
-
dihydrolipoamide dehydrogenase E3 is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, wheras it is bound to the pyruvate dehydrogenase complex through a protein X
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
-
the apicoplast isozyme contains a potential transit peptide, the mitochondrial isozyme contains targeting sequence
phosphoprotein
-
tyrosine-phosphorylated differently concerning time course in the principal piece of the flagella and the acrosome in capacitated spermatozoa, tyrosine-phosphorylation has regulatory function
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, X-ray diffraction structure determination and analysis, small-angle X-ray scattering of the enzyme in solution, measurements in 50 mM Tris buffer, pH 7.5, at 10°C, molecular docking and modeling
-
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
-
sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 7.45, 0.2 M MgCl2, 25% (w/v) PEG 3350 for the wild type enzyme and 1.6 M NaH2PO4/K2HPO4 pH 8.1 plus 2.5 M K2HPO4 for mutant enzyme D444V
-
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
purified enzyme in apoform, and in complexes with Nad+ and NADH, X-ray diffraction structure determination and analysis at 1.35-1.79 A resolution
best results obtained by vapour diffusion method, three-dimensional structure at 2.8 A resolution
-
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PROTEIN VARIANTS
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 20°C lower than the wild-type
E423Q
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423S
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
E423A
-
in 2 M KCl, the mutant is significantly less active than wild-type, decreased Km value for dihydrolipoamide. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
-
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 20°C lower than the wild-type
-
E423Q
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
-
E423S
-
in 2 M KCl, the mutant is significantly less active than wild-type, whereas Km, differences are not significant. The mutant enzyme is not significantly activated by high salt concentrations. In the presence of 2 M KCI the thermal stability of the mutant enzyme is slightly higher than that of the wild-type enzyme
-
A328V
site-directed mutagenesis of the conserved residue, the site-specific dihydrolipoamide dehydrogenase mutant shows a switched kinetic mechanism, it shows a random sequential kinetic mechanism with an interaction factor (alpha) of 8.5. The mutation deteriorates substantially the catalytic power of human E3 enzyme increasing the binding affinity for NAD+ and dihydrolipoamide . The mutation triggers this potential intrinsic property of the enzyme causing the kinetic mechanism of the mutant to switch from a ping-pong mechanism to a random sequential mechanism
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
C50A
site-directed mutagenesis, catalytic efficiency of mutant C50A toward NAD+ decreases 5317fold compared to the wild-type enzyme, the mutation destroys the active disulfide center between Cys45 and Cys50, which restricts the freedom of Cys50
C50T
site-directed mutagenesis, catalytic efficiency of mutant C50A toward NAD+ decreases 2057fold compared to the wild-type enzyme, the mutation destroys the active disulfide center between Cys45 and Cys50, which restricts the freedom of Cys50
D320N
D413A
the mutant shows 85% activity in the forward reaction and 79% activity in the reverse reaction compared to the wild type enzyme
D413N
the mutant shows 119% activity in the forward reaction and 96% activity in the reverse reaction compared to the wild type enzyme
D444V
D473L
-
site-directed mutagenesis, mutant shows about 37fold decreased activity and small conformational changes compared to the wild-type enzyme
DELTAG101
naturally occuring mutation, the mutation is involved in E3 deficiency
E192Q
-
specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced
E340K
E431A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
E457Q
-
molar ratio of FAD to enzyme is 0.9 compared to 1 for the wild-type enzyme, mutation affects the environment surrounding FAD, decrease in efficiency of electron transfer from the reduced flavin to the oxidized substrate
G194C
G426E
naturally occuring mutation, the mutation is involved in E3 deficiency
H329A
site-directed mutagenesis, the kcat value of the mutant is significantly decreased by 24fold as compared to the wild-type, indicating that the mutation severely deteriorates the catalytic power of the enzyme
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
I12T
naturally occuring mutation, the mutation is involved in E3 deficiency
I318T
naturally occuring mutation, the substitution triggers major structural disturbance only at the C-terminus
I445M
I51A
-
mutant with about 100fold reduced activity compared to the wild type enzyme
K37E
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
L99A
the mutation deteriorates the catalytic power of the enzyme substantially
M326V
N286D
N286Q
P154A
the mutation makes enzyme binding to both dihydrolipoamide and NAD+ inefficient
P156A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P303A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P325A
-
mutation of highly conserved resdue in the central domain, about 150fold decrease in kcat value
P355A
the mutation makes enzyme binding to NAD+ substantially less efficient. The catalytic efficiency of the mutant toward NAD+ is decreased by 81% compared to the wild type enzyme
P387A
the mutation deteriorates severely the catalytic power of the enzyme
P423A
the mutation makes enzyme binding to both dihydrolipoamide and NAD+ inefficient
P453L
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
R460G
S456A
-
exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity
S53K/K54S
-
about 25% less bound FAD compared to wild-type, specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced. The catalytic rate constant, turnover number/Km, is significantly lower than wild-type
T148G
specific activity is 76.34% to that of wild-type E3. FAD-content is about 710% that of wild-type E3. Substitution has no effect in the self-dimerization
T148S
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
A48I
-
the mutation decreases the Km for dihydrolipoamide substrate by 3fold compared to the wild type enzyme
A54I
-
the mutation increases the Km for dihydrolipoamide substrate by 1fold and NAD+ by 3fold compared to the wild type enzyme
C15T
-
the mutation increases the Km for dihydrolipoamide substrate by 5fold and NAD+ by 3fold compared to the wild type enzyme
C38G
-
the mutation increases the Km for NAD+ by 9fold without affecting Km for dihydrolipoamide compared to the wild type enzyme
Cys38Gly
-
the substitution does not show any change in Km value for dihydrolipoamide compared to the wild type enzyme
D49G
-
the mutation decreases the Km for dihydrolipoamide substrate by 2fold compared to the wild type enzyme
A181V
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
A290R
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
F269R
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
G312A/L313G/L314P/Q315M
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
L314P
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
N209V
the mutant is less sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
R147T
the mutant is more sensitive to N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid than the wild type enzyme
R347S
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
A181V
-
the mutant is not inhibited by N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamid compared to the wild type enzyme
-
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
-
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
-
I192G
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
V191Y
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
I192G
-
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
-
V191Y
-
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
-
additional information
D320N
48.60% specific activity of the wild type enzyme, 82.7% of FAD content compared to that of the wild-type enzyme
D320N
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
D444V
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 12% of that of the wild type enzyme
D444V
-
shows weak proteolytic activity with mature frataxin substrate, but consistently cleaves mature frataxin to denoted frataxin products with faster kinetics than the wild-type
D444V
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells
D444V
-
the mutation causes microcephaly, blindness, deafness, mild hypertrophic cardiomyopathy, and metabolic acidosis. The substitution leads to compromised enzyme activity (15% of the control)
E340K
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 38% of that of the wild type enzyme
E340K
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells. The mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
G194C
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells
I445M
naturally occuring mutation, the mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
K37E
-
molar ratio of FAD to enzyme is 0.76 compared to 1 for the wild-type enzyme
M326V
naturally occuring mutation, the mutation is involved in E3 deficiency
N286D
30.84% specific activity of the wild type enzyme, 96% of FAD content compared to that of the wild-type enzyme
N286D
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
N286Q
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
P453L
naturally occuring mutation, the mutation significantly stimulates ROS generation of the mutant enzyme, the mutation triggers the oxidative deterioration of the lipoic acid cofactors of both PDHc-E2 and KGDHc-E2 in a yeast model and leads to a great reduction in the respiratory function of the yeast cells. The mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
R447G
-
missense mutation, expressed at 28ºC the mutant exhibits essentially wild-type E3 activity, at 37°C the activity is reduced to 28% of that of the wild type enzyme
R447G
naturally occuring mutation, the mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)
R460G
-
missense mutation, the dissociation constant is three orders of magnitude higher than that of wild-type E3
additional information
generation of DLDH2 enzyme knockout mutant plants, the aos phenotype in mtlpd2-2 is due to disruption of mtLPD2. Mutation of mtLPD2 enhances As(V)-induced changes in metabolite pools, aos phenotype analysis, overview
additional information
-
generation of DLDH2 enzyme knockout mutant plants, the aos phenotype in mtlpd2-2 is due to disruption of mtLPD2. Mutation of mtLPD2 enhances As(V)-induced changes in metabolite pools, aos phenotype analysis, overview
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
-
generation of Pfae3 deletion mutants of Plasmodium falciparum, the gene is replaced by the selectable marker hdhfr after initial positive selection with WR99210 followed by negative selection using 5-fluorocytosine generating the line 3D7DELTAae3, phenotype, overview
additional information
-
deletion of the LPD1 gene prevents oxidative stress in npt1DELTA and bna6DELTA mutants
additional information
-
protein expressed without lipoic acid is indistinguishable from the wild-type protein. The protein without a lipoyl protein domain has a 2-3fold higher turnover number, a lower Ki for NADH, and a higher Ki for lipoamide compared with the other two enzymes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
enzyme loses its activity completely below pH 6 and above pH 11
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
40
-
recombinant enzyme is stable at 30°C upon 30 min of incubation without substrates, but incubation at 40°C and higher temperatures inactivated enzyme activity
55 - 70
the remaining activity after thermal treatment at pH 7.0 for 15 min is 90% at 55°C, 80% at 60°C, 70% at 65 °C, and 45% at 70°C
65
70
75
-
50% loss of activity after 15 min, 50% loss of activity after 20 min in presence of NAD+, 50% loss of activity after less than 1 min in presence of dihydrolipoamide
95
additional information
65
-
the enzyme unfolds irreversibly at heat treatment higher than 65°C
95
-
15 min, in presence of 4 M NaCl, enzyme in crude extract, stable
95
-
15 min, in presence of 4 M NaCl, enzyme in crude extract, stable
additional information
in thepresence of 2 M KCI, the thermal stability properties of mutant enzymes E423S, E423Q and E423A are comparable to those of wild-type, although the mutants appear to be slightly more stable. Mutant enzyme E423D however, is inactivated at temperatures around 20°C lower than for the wild-type. In the absence of salt, similar relative thermostabilities are observed, but both wild-type and mutant enzymes are inactivated at temperatures around 16-18°C lower than in the presence of salt
additional information
-
in thepresence of 2 M KCI, the thermal stability properties of mutant enzymes E423S, E423Q and E423A are comparable to those of wild-type, although the mutants appear to be slightly more stable. Mutant enzyme E423D however, is inactivated at temperatures around 20°C lower than for the wild-type. In the absence of salt, similar relative thermostabilities are observed, but both wild-type and mutant enzymes are inactivated at temperatures around 16-18°C lower than in the presence of salt
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity when the enzyme is frozen at -20°C, and thawed three times
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, -20°C, 100 mM potassium phosphate, 100 mM KCl, pH 7.0, 1 mM EDTA, 50% v/v glycerol, stable for at least 1 year
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on propyllipoamide-glass columns
ammonium sulfate precipitation and Ni-NTA agarose column chromatography
Starkeyomyces koorchalomoides
-
by gel filtration
DEAE-Toyopearl 650 M column chromatography, butyl-Toyopearl 650 M column chromatography, and TSK-gel G3000SW gel filtration
dissociation of the lipoamide dehydrogenase component from the branched-chain alpha-keto acid dehydrogenase complex during purification
-
enzmye from culture supernatant of Clostridium kluyveri is purified using a DEAE-toyopearl column and a TSK-GEL G-3000 column. Recombinant protein is purified using a HiTrap chelating HP column
-
from pyruvate dehydrogenase complex
gel filtration
metal-affinity chromatography and Superdex 200 gel filtration chromatography
Ni-NTA column chromatography
Ni-NTA-agarose resin column chromatography and Superdex 200 gel filtration
presence of dithiothreitol during purification preserves enzymatic activity
-
purified using copper-based metal ion affinity chromatography in the presence of 2 M KCl
recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and hydrophobic interaction chromatography to over 98% purity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain NovaBlue (DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged truncated isozymes from Escherichia coli by nickel affinity chromatography to 98% homogeneity
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration. Purification of native pyruvate and2-oxoglutarate dehydrogenase complexes from strain PA14 by hydroxyapatite chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain XL-1 Blue by nickel affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration
recombinant N-terminally GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
wild-type DLD and mutants purified by nickel affinity chromatography. C-term DLD purified to near homogeneity by a five-step procedure
-
from pyruvate dehydrogenase complex
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bfmBC gene encoding DLD. Ligated into vector pCR2.1, and introduced into Escherichia coli DH5alpha. Insert DNA recovered from the recombinant plasmid ligated into vector pET-28a(+), yielding pET-bfmBC and expressed in Escherichia coli BL21 (DE3)
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex, expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis of both lipdh genes using RT-PCR, expression of the mitochondrial isozyme as GFP-fusion protein giving green fluorescence and of the apicoplast isozyme fused to acyl-carrier-protein resulting in red fluorescence, expression of truncated mitochondrial and apicoplastic isozymes lacking the putative target sequences as His-tagged proteins in Escherichia coli strain BL21-RIL(DE3), the apicoplast isozyme is expressed at very low levels
-
DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Codon Plus RLI cells
expressed in Escherichia coli using the cytoplasmic expression vectors, pET3a and pET3d. Expressed as inclusion bodies and refolded by solubilisation in 8 M urea followed by dilution into a buffer containing 2 M KCl, 0.010 mM FAD, 1 mM NAD+, and 0.3 mM GSSG/3 mM GSH
expression in a strain of Haloferax volcanii lacking dihydrolipoamide dehydrogenase activity
expression in Escherichia coli
expression in Escherichia coli or in Corynebacterium glutamicum, the cloned gene is expressed in Corynebacterium glutamicum cells harbouring the gene on a plasmid shows 12fold higher specific LPD activity when compared to the wild-type strain
gene dld, DNA and amino acid sequence determination and analysis, genotyping
gene dld, located on chromosome 7, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL-1 Blue
gene dld, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha
gene dld, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain XL-1 Blue
gene DLD, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene encoding hDLDH but excluding the N-terminal 1?35 signal peptide region and containing an N-terminal His6-tag, recombinant expression in Escherichia coli strain BL21(DE3)
gene lpd2, recombinant expression of GUS-linked enzyme in Arabidopsis thaliana ecotype Col-0 in cotyledons, rosette leaves and roots (in the cap of the established lateral roots, but not in the cap of the main roots) via transformation by Agrobacterium tumefaciens strain GV3101
gene lpd3, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene lpdG, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene lpdV, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Pfae3, recombinant expression of His-tagged enzyme in Escherichia coli strain NovaBlue (DE3), transfection of pCC1-Pfae3 Plasmodium falciparum 3D7 erythrocytic stages
-
His-tagged wild-type and mutant proteins overexpressed in Escherichia coli
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
overexpressed in the parent organism by using the halophilic archaeal rRNA promoter
recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strain BL21(DE3)
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
-
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
-
ligated into vector pET-28a(+) and expressed in Escherichia coli BL21(DE3) as an N-terminal 6 x His-tag
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression level of the enzyme is significantly lower in the head and neck cancer than in normal cells
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the full-length isoform of dihydrolipoamide dehydrogenase is induced by Nutin-3, while the shorter isoform of dihydrolipoamide dehydrogenase is downregulated by Nutlin-3, immunochemical analysis of dihydrolipoamide dehydrogenase protein levels after MDM2 perturbation, overview. Depletion of MDM2 using siRNA elevates dihydrolipoamide dehydrogenase in Nutlin-3-treated cells. An increase in MDM2/dihydrolipoamide dehydrogenase complexes in the nucleus is further enhanced by the nuclear export inhibitor Leptomycin B
the full-length isoform of dihydrolipoamide dehydrogenase is induced by Nutin-3, while the shorter isoform of dihydrolipoamide dehydrogenase is downregulated by Nutlin-3, immunochemical analysis of dihydrolipoamide dehydrogenase protein levels after MDM2 perturbation, verview
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inactivation of the enzyme by guanidine-HCl is reversible by its removal
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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development of a blue native-PAGE-based method for isolation of enzymatically active DLDH from animal tissues and visualization as well as quantification of its diaphorase activity using the NADH/nitroblue tetrazolium detection system
degradation
diagnostics
drug development
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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 pyruvate dehydrogenase complex, PDC. Plasmodium PDC is essential for parasite survival in the mosquito vector and for late liver stage development in the human host, suggesting its suitability as a target for intervention strategies against malaria
medicine
additional information
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
-
shows flavin reductase activity with moderate diaphorase activity
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
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
shows NADH-dependent tellurite reductase activity in vitro
degradation
-
decreased activity of DLDH induced by valproic acid metabolites may, at least in part, account for the impaired rate of oxygen consumption and ATP synthesis in mitochondria if 2-oxoglutarate or glutamate are used as respiratory substrates, thus limiting the flux of these substrates through the citric acid cycle
degradation
T148 is not important to E3 catalytic function, whereas R281 plays a role in the catalytic function of E3
diagnostics
-
Bacillus sphaericus DLD-diaphorase exhibits considerable potential to be used as a component of diagnostic tests for the quantification of metabolites
diagnostics
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Bacillus sphaericus DLD-diaphorase exhibits considerable potential to be used as a component of diagnostic tests for the quantification of metabolites
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medicine
-
mutations of the enzyme cause the often-fatal human disease known as E3 deficiency
medicine
-
direct involvement of LpdC in the prolonged retention of coronin-1 on the phagosome, thus promoting phagosome maturation arrest. Under the influence of IFNgamma, LRG-47 is recruited to the phagosome and mediates dislocation of coronin-1 leading ultimately to phagosome acidification and recruitment of lysosomal vacuoles and phagolyosome fusion
medicine
-
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
-
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
-
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
medicine
-
dihydrolipoyl dehydrogenase is an important source of reactive oxygen species leading to life span limitation
medicine
-
NADH diaphorase staining can establish tissue non-viability after radiofrequency ablation, but the timing of staining after treatment must be considered when interpreting results to avoid false positive tests. Tissue that is apparently viable by NADH diaphorase staining within 2.5 hours of radiofrequency ablation may in fact have been ablated
medicine
-
brain DLDH expression and activity undergo independent postnatal maturational increases. Senescence does not confer any detectable change in the activity of DLDH or its susceptibility to inactivation by mitochondrial oxidative stress
medicine
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
medicine
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due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues
medicine
due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues
medicine
the enzyme is a DNA chelating agent. Enzyme binding to DNA presents a moonlight activity which may be used for DNA alkylating in cancer treatment
medicine
-
Arg-Gly-Asp-modified enzyme enhances the adhesion of bone forming cells to titanium dioxide implant surfaces
medicine
-
lipoamide dehydrogenase activity and metallothionein levels may be critical for dopaminergic neuronal survival in Parkinson's disease. 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine can affect the lipoamide dehydrogenase activity and metallothionein content to exert its neurotoxicity
-
medicine
-
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
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medicine
-
due to its TiO2 binding ability, the enzyme may serve as a molecular bridge between Ti-based medical structures and human tissues
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additional information
high stability of rBfmBC may make it useful for practical use
additional information
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high stability of rBfmBC may make it useful for practical use
additional information
metabolic context(s) of DLDHs remains an open question
additional information
-
metabolic context(s) of DLDHs remains an open question
additional information
-
a mutation in LPD leads to a pyruvate dehydrogenase complex that is less sensitive to inhibition by NADH, allowing the enzyme to function in an anaerobic culture, which changes the fermentation profile of the mutant. Presence and functional activity of such an NADH-insensitive pyruvate dehydrogenase may have significant unexplored physiological and biotechnological applications
additional information
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the lipoyl protein domain (but not lipoic acid alone) plays a regulatory role in the enzymatic characteristics of pneumococcal DLDH
EXTERNAL LINKS (specific for EC-Number 1.8.1.4)
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Release 2026.1 (March 2026)
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