Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase and Organism(s) Homo sapiens and UniProt Accession P09622

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-

r

dihydrolipoamide + NAD+

lipoamide + NADH + H+

7 entries

dihydrolipoic acid + NAD+

lipoic acid + NADH + H+

-

765736

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?

lipoamide + NADH

dihydrolipoamide + NAD+

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r

lipoamide + NADH + H+

dihydrolipoamide + NAD+

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-

?

lipoic acid + NADH

dihydrolipoic acid + NAD+

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r

protein N6-(lipoyl)lysine + NADH + H+

protein N6-(dihydrolipoyl)lysine + NAD+

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r

dihydrolipoamide + NAD+

lipoamide + NADH

dihydrolipoamide + NAD+

lipoamide + NADH + H+

lipoamide + NADH

dihydrolipoamide + NAD+

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?

mature frataxin + NADH

denoted frataxin + NAD+

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cleavage by C-term DLD

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?

protein N6-(dihydrolipoyl)lysine + NAD+

protein N6-(lipoyl)lysine + NADH + H+

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764703

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?

additional information

?

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3 entries

dihydrolipoamide + NAD+

lipoamide + NADH + H+

protein N6-(lipoyl)lysine + NADH + H+

protein N6-(dihydrolipoyl)lysine + NAD+

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r

dihydrolipoamide + NAD+

lipoamide + NADH

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?

dihydrolipoamide + NAD+

lipoamide + NADH + H+

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r

protein N6-(dihydrolipoyl)lysine + NAD+

protein N6-(lipoyl)lysine + NADH + H+

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764703

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?

additional information

?

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FAD

flavin

dependent on

NAD+

NADH

FAD

flavin

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flavoprotein

NAD+

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393971, 393993, 394003, 394004, 659101, 672869, 673943, 674382, 674759, 675350, 677161, 691569, 711099, 764703

NADH

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5-methoxyindole-2-carboxylic acid

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763920

diisopropyl fluorophosphate

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fully inhibits activity of the C-term protein

additional information

Nutlin-3 inhibits mitochondrial activity

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0.027 - 1.21

dihydrolipoamide

28 entries

0.05 - 0.56

Lipoamide

0.024 - 1.3

NAD+

27 entries

0.04 - 0.24

NADH

0.05 - 43.6

dihydrolipoamide

10 entries

0.31 - 5

Lipoamide

0.06 - 0.55

NAD+

9 entries

0.071 - 0.13

NADH

additional information

6 entries

-

0.42 - 1309

dihydrolipoamide

25 entries

67 - 519

Lipoamide

0.42 - 899

NAD+

10 entries

6 - 1032

dihydrolipoamide

6 entries

14.4 - 649

Lipoamide

6.75 - 574

NAD+

3 entries

19.8 - 340

NADH

3 entries

additional information

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-

52 - 1405

dihydrolipoamide

6 entries

0.89 - 4732

NAD+

0.00196

diisopropyl fluorophosphate

Homo sapiens

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143.1

mutant N286Q

179.6

mutant N286D

283.1

mutant D320N

586.5

wild-type

16.6

-

purified recombinant mutant D473L

280

-

purified recombinant mutant T44V enzyme

additional information

7.5

assay at

8

assay at

742221, 743050, 743051, 743052

8

-

assay at

659099, 659101

22

assay at room temperature

37

assay at

742221, 743050, 743051, 743052

37

head and neck cancer cell

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assay at

immunochemical analysis of dihydrolipoamide dehydrogenase protein levels

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evolution

malfunction

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

malfunction

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pathogenic mutations of LADH cause severe metabolic disturbances, called E3 deficiency that often involve cardiological and neurological symptoms and premature death. Some of the known pathogenic mutations augment the reactive oxygen species (ROS) generation capacity of LADH, which may contribute to the clinical presentations. Structural changes are likely to turn the physiological LADH conformation to its ROS-generating conformation

physiological function

additional information

5 entries

P09622 pBLAST

DLDH_HUMAN

509

0

54177

Swiss-Prot

Show Sequence

Mitochondrion (Reliability: 2)

110000

55000

2 * 55000, SDS-PAGE

50216

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2 * 50216, amino acid sequence calculation

dimer

homodimer

?

-

dimer

homodimer

additional information

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the homodimeric enzyme is the E3 component of 2-ketoacid dehydrogenase multienzyme complex

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

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674759

hanging drop vapour diffusion method

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675350, 677161

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

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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

742221

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

743051

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

substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 18%. The binding affinities of the mutant to the di-domain of the E3-binding protein are severely reduced

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

DELTAG101

naturally occuring mutation, the mutation is involved in E3 deficiency

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

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

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

L99A

the mutation deteriorates the catalytic power of the enzyme substantially

765208

M326V

naturally occuring mutation, the mutation is involved in E3 deficiency

N286D

N286Q

P154A

the mutation makes enzyme binding to both dihydrolipoamide and NAD+ inefficient

765207

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

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

765209

P387A

the mutation deteriorates severely the catalytic power of the enzyme

765210

P423A

the mutation makes enzyme binding to both dihydrolipoamide and NAD+ inefficient

765207

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)

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

R447G

naturally occuring mutation, the mutant shows greatly enhanced exposure or dynamics of the C-terminus (fragments 465-474, 469-474)

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

Y438A

substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 9%. The binding affinities of the mutant to the di-domain of the E3-binding protein are severely reduced and binding of is accompanied by an unfavorable enthalpy change and a large positive entropy change

Y438H

substitutions has no large effects on E3 activity when measured in its free form. However, when reconstituted in the complex, the pyruvate dehydrogenase activity is reduced to 20%. The binding affinities of the mutant to the di-domain of the E3-binding protein ire severely reduced

A1444G

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substitution located in exon 13 leading to 20% of wild type activity

673943

C45S

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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

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purification of the Tyr-45 mutant is not successful. Recombinant human E3 becomes too unstable to be easily obtained from Escherichia coli

D413A

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the mutant shows 85% activity in the forward reaction and 79% activity in the reverse reaction compared to the wild type enzyme

D413N

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the mutant shows 119% activity in the forward reaction and 96% activity in the reverse reaction compared to the wild type enzyme

D444V

D473L

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site-directed mutagenesis, mutant shows about 37fold decreased activity and small conformational changes compared to the wild-type enzyme

E192Q

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specific activity is markedly decreased, less than 5% of the wild-type activity, Km-values for lipoamide and dihydrolipoamide are markedly reduced

E340K

E431A

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exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity

E457Q

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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

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mutation affecting the ability of FAD, NAD+, or NADH to bind to E3

H348A

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the mutant shows 60% activity in the forward reaction and 66% activity in the reverse reaction compared to the wild type enzyme

H348L

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the mutant shows 65% activity in the forward reaction and 74% activity in the reverse reaction compared to the wild type enzyme

H450A

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shows an increase in proteolytic activity as compared with the wild-type

H452Q

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molar ratio of FAD to enzyme is 0.94 compared to 1 for the wild-type enzyme, no production of NADH when the enzyme is reduced by dihydrolipoamide, transfer of electrons from the substrate dihydrolipoamide to NAD+ is extremely low

I358T

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mutation affecting the ability of FAD, NAD+, or NADH to bind to E3

I51A

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mutant with about 100fold reduced activity compared to the wild type enzyme

674382

K37E

K54E

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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

M326V

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mutation affecting the ability of FAD, NAD+, or NADH to bind to E3

P325A

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mutation of highly conserved resdue in the central domain, about 150fold decrease in kcat value

724686

P453L

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causes E3 deficiency

P453V

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1650fold lower specific activity compared to the wild type enzyme

672869

R447A

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the mutant shows 110% activity in the forward reaction and 122% activity in the reverse reaction compared to the wild type enzyme

R447G

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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

677161

R460G

S456A

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exhibits very similar expression levels and purification yields as the wild-type, but abolishes the proteolytic activity

S456A/D444V

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low levels of residual activity

S53K/K54S

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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

T44V

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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

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mutation of highly conserved residue. kinetic parameters similar to wild-type

724686

Y438A

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the mutant shows 100% activity in the forward reaction and 91% activity in the reverse reaction compared to the wild type enzyme

Y438F

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the mutant shows 100% activity in the forward reaction and 112% activity in the reverse reaction compared to the wild type enzyme

Y438H

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the mutant shows 99% activity in the forward reaction and 92% activity in the reverse reaction compared to the wild type enzyme

additional information

-

deletion mutant DELTAG101 causes E3 deficiency

gel filtration

Ni-NTA His-Bind resin column chromatography

765207, 765208

nickel affinity column chromatography

765209

recombinant His-tagged E3 wild-type and mutant proteins

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

743050, 743051

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

Strep-Tactin Sepharose column chromatography

wild-type and mutant proteins, highly purified

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672869, 691569, 764703

Ni-NTA agarose column chromatography, gel filtration

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Ni-NTA resin column chromatography and gel filtration

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nickel iminodiacetic acid Sepharose 6B column chromatography

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674382

recombinant D473L mutant from Escherichia coli to homogeneity

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recombinant mutant T44V from Escherichia coli strain XL1-Blue

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Sephacryl S-100 column gel filtration

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677161

Superdex HR-200 gel filtration

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674759

wild-type and mutant enzymes K37E, H452Q and E457Q

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wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q

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wild-type DLD and mutants purified by nickel affinity chromatography. C-term DLD purified to near homogeneity by a five-step procedure

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expressed in Escherichia coli

674943, 765209

expressed in Escherichia coli DH5alpha cells

765207, 765208

expressed in Escherichia coli JM83 cells

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

743051

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)

His-tagged wild-type and mutant proteins overexpressed in Escherichia coli

mutants cloned into pQE-9 vector

recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strain BL21(DE3)

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expressed in Escherichia coli

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674382, 674759, 675350, 764703

expressed in Escherichia coli BL21 cells

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expressed in Escherichia coli XL1-Blue

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expression of D473L mutant in Escherichia coli strain XL1-Blue

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expression of mutant T44V in Escherichia coli strain XL1-Blue

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wild-type and mutant enzymes K37E, H452Q and E457Q

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wild-type and mutant enzymes K37E, H452Q and E457Q, overexpression in Escherichia coli

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wild-type and mutant enzymes K54E, S53K54-K53S54 and E192Q, overexpression in Escherichia coli

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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

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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

the expression level of the enzyme is significantly lower in the head and neck cancer than in normal cells

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degradation

medicine

degradation

medicine

Carothers, D.J.; Pons, G.; Patel, M.S.

Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases

Arch. Biochem. Biophys.

268

409-425

1989

Ascaris suum, Azotobacter vinelandii, Bacillus subtilis, Bos taurus, Escherichia coli, Geobacillus stearothermophilus, Halobacterium salinarum, Homo sapiens, Pisum sativum, Pseudomonas aeruginosa, Pseudomonas putida, Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces pastorianus, Sus scrofa

2643922

393993

Williams, C.H.

Flavin-containing dehydrogenases

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

13

89-173

1976

Azotobacter agilis, Azotobacter vinelandii, Bacillus subtilis, Bos taurus, Brassica oleracea, Enterococcus faecalis, Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli Crookes, Escherichia coli M191-6, Globisporangium ultimum, Homo sapiens, Leuconostoc mesenteroides, Mycobacterium tuberculosis, Neurospora crassa, Parvimonas micra, Phytophthora erythroseptica, Pichia kudriavzevii, Proteus vulgaris, Pseudomonas fluorescens, Rattus norvegicus, Saccharomyces cerevisiae, Serratia marcescens, Spinacia oleracea, Squalus acanthias, Sus scrofa

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Liu, T.C.; Korotchkina, L.G.; Hyatt, S.L.; Vettakkorumakankav, N.N.; Patel, M.S.

Spectroscopic studies of the characterization of recombinant human dihydrolipoamide dehydrogenase and its site-directed mutants

J. Biol. Chem.

270

15545-15550

1995

Homo sapiens

7797549

Liu, T.C.; Soo Hong, Y.; Korotchkina, L.G.; Vettakkorumakankav, N.N.; Patel, M.S.

Site-directed mutagenesis of human dihydrolipoamide dehydrogenase: role of lysine-54 and glutamate-192 in stabilizing the thiolate-FAD intermediate

Protein Expr. Purif.

16

27-39

1999

Homo sapiens

10336857

658466

Wu, Y.Y.; Hsu, T.C.; Chen, T.Y.; Liu, T.C.; Liu, G.Y.; Lee, Y.J.; Tsay, G.J.

Proteinase 3 and dihydrolipoamide dehydrogenase (E3) are major autoantigens in hepatitis C virus (HCV) infection

Clin. Exp. Immunol.

128

347-352

2002

Homo sapiens

11985526

Kim, H.

Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD-binding region to valine

J. Biochem. Mol. Biol.

35

437-441

2002

Homo sapiens

12297006

Kim, H.

Asparagine-473 residue is important to the efficient function of human dihydrolipoamide dehydrogenase

J. Biochem. Mol. Biol.

38

248-252

2005

Homo sapiens

15826505

672869

Kim, H.

Examination of the importance of Pro-453 in human dihydrolipoamide dehydrogenase predicted from the three-dimensional structure

Bull. Korean Chem. Soc.

27

819-820

2006

Homo sapiens

-

673943

Odievre, M.H.; Chretien, D.; Munnich, A.; Robinson, B.H.; Dumoulin, R.; Masmoudi, S.; Kadhom, N.; Roetig, A.; Rustin, P.; Bonnefont, J.P.

A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency

Hum. Mutat.

25

323-324

2005

Homo sapiens

15712224

674382

Kim, H.

Activity of human dihydrolipoamide dehydrogenase is largely reduced by mutation at isoleucine-51 to alanine

J. Biochem. Mol. Biol.

39

223-227

2006

Homo sapiens

16584639

674759

Ciszak, E.M.; Makal, A.; Hong, Y.S.; Vettaikkorumakankauv, A.K.; Korotchkina, L.G.; Patel, M.S.

How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex

J. Biol. Chem.

281

648-655

2006

Homo sapiens

16263718

Wang, Y.C.; Wang, S.T.; Li, C.; Liu, W.H.; Chen, P.R.; Chen, L.Y.; Liu, T.C.

The role of N286 and D320 in the reaction mechanism of human dihydrolipoamide dehydrogenase (E3) center domain

J. Biomed. Sci.

14

203-210

2007

Homo sapiens (P09622), Homo sapiens

17171578

Brautigam, C.A.; Chuang, J.L.; Tomchick, D.R.; Machius, M.; Chuang, D.T.

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations

J. Mol. Biol.

350

543-552

2005

Homo sapiens

15946682

677161

Brautigam, C.A.; Wynn, R.M.; Chuang, J.L.; Machius, M.; Tomchick, D.R.; Chuang, D.T.

Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex

Structure

14

611-621

2006

Homo sapiens

16442803

Kim, H.

Site-specific modifications of the Cys-45 residue in human dihydrolipoamide dehydrogenase to Ser and Tyr

Bull. Korean Chem. Soc.

28

907-908

2007

Homo sapiens

-

Wang, Y.C.; Wang, S.T.; Li, C.; Chen, L.Y.; Liu, W.H.; Chen, P.R.; Chou, M.C.; Liu, T.C.

The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase

J. Biomed. Sci.

15

37-46

2008

Homo sapiens (P09622), Homo sapiens

17960497

694356

Brown, A.M.; Gordon, D.; Lee, H.; Wavrant-De Vrieze, F.; Cellini, E.; Bagnoli, S.; Nacmias, B.; Sorbi, S.; Hardy, J.; Blass, J.P.

Testing for linkage and association across the dihydrolipoyl dehydrogenase gene region with Alzheimers disease in three sample populations

Neurochem. Res.

32

857-869

2007

Homo sapiens

17342416

Babady, N.E.; Pang, Y.P.; Elpeleg, O.; Isaya, G.

Cryptic proteolytic activity of dihydrolipoamide dehydrogenase

Proc. Natl. Acad. Sci. USA

104

6158-6163

2007

Homo sapiens, Mus musculus, Sus scrofa

17404228

Park, Y.H.; Patel, M.S.

Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex

Biochem. Biophys. Res. Commun.

395

416-419

2010

Homo sapiens

20385101

Ambrus, A.; Torocsik, B.; Adam-Vizi, V.

Periplasmic cold expression and one-step purification of human dihydrolipoamide dehydrogenase

Protein Expr. Purif.

63

50-57

2009

Homo sapiens (P09622), Homo sapiens

18845259

724686

Kim, H.

Characterization of two site-specific mutations in human dihydrolipoamide dehydrogenase

Bull. Korean Chem. Soc.

34

1621-1622

2013

Homo sapiens

-

Ambrus, A.; Adam-Vizi, V.

Molecular dynamics study of the structural basis of dysfunction and the modulation of reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase

Arch. Biochem. Biophys.

538

145-155

2013

Homo sapiens

24012808

741807

Ambrus, A.; Mizsei, R.; Adam-Vizi, V.

Structural alterations by five disease-causing mutations in the low-pH conformation of human dihydrolipoamide dehydrogenase (hLADH) analyzed by molecular dynamics - implications in functional loss and modulation of reactive oxygen species generation by pa

Biochem. Biophys. Rep.

2

50-56

2015

Homo sapiens (P09622), Homo sapiens

27544700

Ambrus, A.; Wang, J.; Mizsei, R.; Zambo, Z.; Torocsik, B.; Jordan, F.; Adam-Vizi, V.

Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry implications for the structural basis of E3 deficiency

Biochim. Biophys. Acta

1862

2098-2109

2016

Homo sapiens (P09622), Homo sapiens

27544700

Moxley, M.A.; Beard, D.A.; Bazil, J.N.

A pH-dependent kinetic model of dihydrolipoamide dehydrogenase from multiple organisms

Biophys. J.

107

2993-3007

2014

Spinacia oleracea (A0A0K9R8G5), Spinacia oleracea, Homo sapiens (P09622), Homo sapiens, Escherichia coli (P0A9P0), Escherichia coli

25517164

742221

Kim, H.

Characterization of site-specific human dihydrolipoamide dehydrogenase mutant with a switched kinetic mechanism

Bull. Korean Chem. Soc.

35

1603-1604

2014

Homo sapiens (P09622)

-

Kim, H.

Characterization of site-specific mutations affecting the catalytic efficiency of human dihydrolipoamide dehydrogenase toward NAD+

J. Korean Chem. Soc.

59

183-187

2015

Homo sapiens (P09622)

-

743051

Kim, H.

Characterization of site-specific mutations in human dihydrolipoamide dehydrogenase significantly destabilizing the transition state of the enzyme catalysis

J. Korean Chem. Soc.

59

344-348

2015

Homo sapiens (P09622)

-

Kim, H.

Characterization of human dihydrolipoamide dehydrogenase mutant with significantly decreased catalytic power

J. Korean Chem. Soc.

60

378-382

2016

Homo sapiens (P09622)

-

Dayan, A.; Babin, G.; Ganoth, A.; Kayouf, N.S.; Nitoker Eliaz, N.; Mukkala, S.; Tsfadia, Y.; Fleminger, G.

The involvement of coordinative interactions in the binding of dihydrolipoamide dehydrogenase to titanium dioxide-Localization of a putative binding site

J. Mol. Recognit.

30

e2617

2017

Rhodococcus ruber, Homo sapiens (P09622), Homo sapiens, Rhodococcus ruber GIN1

28247484

Way, L.; Faktor, J.; Dvorakova, P.; Nicholson, J.; Vojtesek, B.; Graham, D.; Ball, K.L.; Hupp, T.

Rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3

Proteomics

16

2327-2344

2016

Homo sapiens (P09622)

27273042