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• • Molecular Structure
  • Sum Formula
  • BRENDA Name
  • Synonyms
  • InChIKey
  • Pathways
• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
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Ligand Lipoamide

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for Lipoamide

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.104

pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2

348976, 348956, 348980, 348970, 348978, 348928

-

1.2.1.105

2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2

349038, 349042, 349036, 349018, 348910

-

1.2.4.1

pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2

348922, 348955, 348981, 348974, 348936, 348949, 348968

-

1.2.4.2

2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2

348999

-

1.8.1.4

alpha-lipoamide + NADH + H+ = dihydrolipoamide + NAD+

724002

-

1.8.1.4

lipoamide + NADH + H+ = dihydrolipoamide + NAD+

742126

-

1.8.1.4

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.4

dihydrolipoamide + NAD = lipoamide + NADH + H+

-

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH

-

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH + H+

-

-

1.8.1.4

3 entries

Substrate in Enzyme-catalyzed Reactions (22 results)

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Show Substrate (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.28

lipoamide + H2O2 = ? + H2O

754090

-

1.2.1.104

pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2

348976, 687812, 348956, 348980, 348970, 348978, 348928

-

1.2.1.105

2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2

348914, 349004, 349020, 349021, 349022, 349029, 349043, 349038, 349006, 349007, 349034, 349035, 349036, 349037, 348910, 349001, 349005, 349014, 349023, 349026, 349027, 349028, 349033, 349030, 349032, 349042, 349017, 349003, 349015, 349008, 349040, 349002, 349018, 349044, 349031, 349019, 349024, 349025

-

1.2.4.1

alpha-ketobutyrate + lipoamide = S-propionyldihydrolipoamide + CO2

348974

-

1.2.4.1

pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2

685585, 684365, 348922, 348951, 686469, 348955, 348981, 348974, 348936, 348949, 348968

-

1.2.4.1

2 entries

1.2.4.2

2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO2

699660, 348998, 349010, 348982, 349041, 348999, 349011, 349013, 349009, 348997, 349039, 349000

-

1.4.4.2

glycine + lipoamide = ?

673411

-

1.6.2.6

NADH + lipoamide = NAD+ + ?

394002

-

1.6.2.6

NADH + lipoamide = NAD+ + lipoamide

394513

-

1.8.1.4

(R,S)-lipoamide + NADH + H+ = dihydrolipoamide + NAD+

394011

-

1.8.1.4

alpha-lipoamide + NADH + H+ = dihydrolipoamide + NAD+

724002

-

1.8.1.4

alpha-lipoamide + NADH = dihydrolipoamide + NAD+

711320

-

1.8.1.4

DL-alpha-lipoamide + NADH = dihydrolipoamide + NAD+

713314

-

1.8.1.4

DL-lipoamide + NADH = DL-dihydrolipoamide + NAD+

713453

-

1.8.1.4

lipoamide + 3-acetylpyridine adenine dinucleotide = dihydrolipoamide + ?

394006

-

1.8.1.4

lipoamide + NADH + H+ = dihydrolipoamide + NAD+

673190, 742126, 674943

-

1.8.1.4

lipoamide + NADH = dihydrolipoamide + NAD+

694854, 659167, 392950, 693005, 658799, 692858, 394002, 691392, 713461, 674943, 712521, 692385

-

1.8.1.4

lipoamide + nicotinamide hypoxanthine dinucleotide = dihydrolipoamide + ?

394006

-

1.8.1.4

lipoamide + thio-NADH = dihydrolipoamide + thio-NAD+

394006

-

1.8.1.9

lipoamide + NADPH + H+ = ?

725059

-

1.8.1.9

lipoamide + NADPH + H+ = dihydrolipoamide + NADP+

698965

-

1.8.1.9

lipoamide disulfide + NADPH + H+ = lipoamide + NADP+

742565

-

1.6.2.6

2 entries

1.8.1.4

10 entries

1.8.1.9

3 entries

Product in Enzyme-catalyzed Reactions (11 results)

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Show Product (11 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.28

cumene hydroperoxide + dihydrolipoamide = 2-phenylpropan-2-ol + lipoamide

-

-

1.11.1.28

H2O2 + dihydrolipoamide = H2O + lipoamide

-

-

1.11.1.28

linoleic acid hydroperoxide + dihydrolipoamide = ? + lipoamide

-

-

1.11.1.28

tert-butyl hydroperoxide + dihydrolipoamide = tert-butanol + lipoamide

-

-

1.11.1.28

4 entries

1.6.2.6

NADH + lipoamide = NAD+ + lipoamide

394513

-

1.8.1.4

dihydrolipoamide + NAD = lipoamide + NADH + H+

-

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH

-

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH + H+

-

-

1.8.1.4

dihydrolipoamide + NADP+ = lipoamide + NADPH

393964

-

1.8.1.9

lipoamide disulfide + NADPH + H+ = lipoamide + NADP+

-

-

1.8.1.9

oxidized lipoamide + NADPH = lipoamide disulfide + NADP+

-

-

1.8.1.4

4 entries

1.8.1.9

2 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.4.4

the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1-(thiamine diphosphate)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH

349045

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.21

binds three-fold more weakly than D,L-lipoic acid, competitive

667913

-

1.8.1.4

-

693005

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (26 results)

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Show Turnover Number (26 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.11.1.28

90.9

-

pH 7.4, 37°C

754090

1.4.4.2

0.602

-

kinetic parameter for L protein

673411

1.4.4.2

6.08

-

kinetic parameter for L protein

673411

1.6.2.6

31

-

recombinant enzyme

394513

1.6.2.6

392

-

recombinant FLbR-2

394002

1.8.1.4

14.4

-

mutant enzyme S53K/K54S

394004

1.8.1.4

23

-

mutant enzyme K54E

394004

1.8.1.4

67

-

mutant D320N

674943

1.8.1.4

67

-

mutant enzyme D320N

674943

1.8.1.4

81.3

-

mutant enzyme E192Q

394004

1.8.1.4

88

-

-

394009

1.8.1.4

97

-

pH 7.0, 25°C, recombinant His-tagged enzyme

742126

1.8.1.4

134

-

mutant enzyme N286D

674943

1.8.1.4

134

-

mutant N286D

674943

1.8.1.4

135.5

337

pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions

656835

1.8.1.4

148

-

mutant enzyme N286Q

674943

1.8.1.4

148

-

mutant N286Q

674943

1.8.1.4

190

-

-

394011

1.8.1.4

519

-

wild type enzyme

674943

1.8.1.4

519

-

wild-type

674943

1.8.1.4

649

-

wild-type enzyme

394004

1.8.1.9

1.6

-

isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C

725059

1.8.1.9

2

3.7

wild type enzyme, in TE buffer, at 20°C

698965

1.8.1.9

3.3

-

isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C

725059

1.8.1.9

27.6

-

mutant enzyme Y116I, in TE buffer, at 20°C

698965

1.8.1.9

31.2

-

mutant enzyme Y116T, in TE buffer, at 20°C

698965

1.4.4.2

2 entries

1.6.2.6

2 entries

1.8.1.4

16 entries

1.8.1.9

5 entries

K_M Value (37 results)

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Show KM Value (37 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.11.1.28

0.04446

-

pH 7.4, 37°C

754090

1.4.4.2

0.043

-

the apparent Km-value of rTvL for binding the free lipoamide

673411

1.6.2.6

0.716

-

lipoamide-dependent NADH oxidation

394513

1.6.2.6

3.381

-

recombinant FLbR-2

394002

1.8.1.4

0.05

-

mutant enzyme N286Q

674943

1.8.1.4

0.05

-

mutant N286Q

674943

1.8.1.4

0.07

-

mutant enzyme N286D

674943

1.8.1.4

0.07

-

mutant N286D

674943

1.8.1.4

0.31

-

mutant enzyme E192Q

394004

1.8.1.4

0.37

-

-

394009

1.8.1.4

0.42

-

-

691392

1.8.1.4

0.46

-

mutant D320N

674943

1.8.1.4

0.46

-

mutant enzyme D320N

674943

1.8.1.4

0.5

-

-

394011

1.8.1.4

0.56

-

reaction with 3-acetylpyridine adenine dinucleotide

394006

1.8.1.4

0.56

-

wild type enzyme

674943

1.8.1.4

0.56

-

wild-type

674943

1.8.1.4

0.63

-

mutant enzyme S53K/K54S

394004

1.8.1.4

0.841

-

pH 7.0, 25°C, recombinant His-tagged enzyme

742126

1.8.1.4

0.87

-

pH 8.0, 25°C, mitochondrial isozyme

656835

1.8.1.4

1.26

-

-

692385

1.8.1.4

1.3

-

-

394007

1.8.1.4

2.25

-

wild-type enzyme

394004

1.8.1.4

3.3

-

in the presence of 0.2 mM NAD+, in 50 mM potassium phosphate buffer (pH 6.0), at 25°C

712521

1.8.1.4

3.38

-

-

394002

1.8.1.4

3.63

-

in 0.1 mM Tris-HCl (pH 7.0), 0.0005 mM EDTA, 0.01 mM beta2-mercaptoethanol, at 37°C

711320

1.8.1.4

3.7

-

-

486168

1.8.1.4

5

-

-

393962

1.8.1.4

5

-

mutant enzyme K54E

394004

1.8.1.4

5.8

-

reaction with thio-NADH

394006

1.8.1.4

6.4

-

reaction with nicotinamide hypoxanthine dinucleotide

394006

1.8.1.4

16

-

reaction with NADH

394006

1.8.1.9

0.0019

-

isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C

725059

1.8.1.9

0.0043

-

isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C

725059

1.8.1.9

2.89

-

wild type enzyme, in TE buffer, at 20°C

698965

1.8.1.9

3.68

-

mutant enzyme Y116I, in TE buffer, at 20°C

698965

1.8.1.9

5.59

-

mutant enzyme Y116T, in TE buffer, at 20°C

698965

1.6.2.6

2 entries

1.8.1.4

28 entries

1.8.1.9

5 entries

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.1.4

0.0488

-

recombinant DLDH expressed without lipoic acid, in the presence of 4 mM NAD+

693005

1.8.1.4

0.0566

-

recombinant DLDH, in the presence of 4 mM NAD+

693005

1.8.1.4

0.1899

-

recombinant DLDH expressed without lipoic acid, in the presence of 1.5 mM dihydrolipoamide

693005

1.8.1.4

0.1953

-

recombinant DLDH, in the presence of 1.5 mM dihydrolipoamide

693005

1.8.1.4

0.349

-

recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 4 mM NAD+

693005

1.8.1.4

0.8793

-

recombinant DLDH expressed without without a lipoyl protein domain, in the presence of 1.5 mM dihydrolipoamide

693005

1.8.1.4

6 entries

References & Links

Literature References (103)

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Show Reference (103 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

348910

-

The mammalian 2-oxoacid dehydrogenases: a complex family

1986

Yeaman, S.J.

Trends Biochem. Sci.

11

293-296

348914

-

Multienzyme complexes

1970

Reed, L.J.; Cox, D.J.

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

1

213-240

348922

2748588

Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit

1989

Ho, L.; Wexler, I.D.; Liu, T.C.; Thekkumara, T.J.; Patel, M.S.

Proc. Natl. Acad. Sci. USA

86

5330-5334

348928

-

Purification of the chloroplast pyruvate dehydrogenase complex from spinach and maize mesophyll

1986

Treede, J.; Heise, K.P.

Z. Naturforsch. C

41

1011-1017

348936

16664100

Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex

1985

Camp, P.J.; Randall, D.D.

Plant Physiol.

77

571-577

348949

7144582

Pyruvate dehydrogenase complex from Hansenula

1982

Harada, T.; Hirabayashi, T.

Methods Enzymol.

89

420-423

348951

-

Pyruvate dehydrogenase complex from broccoli and cauliflower

1982

Randall, D.D.

Methods Enzymol.

89

408-414

348955

7144580

Pyruvate dehydrogenase complex from bovine kidney and heart

1982

Pettit, F.H.; Reed, L.J.

Methods Enzymol.

89

376-386

348956

7005225

Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli

1981

Bisswanger, H.

J. Biol. Chem.

256

815-822

348968

227453

Purification and properties of the Ascaris pyruvate dehydrogenase complex

1979

Komuniecki, R.; Komuniecki, P.R.; Saz, H.J.

Biochim. Biophys. Acta

571

1-11

348970

13724

Purification and characterization of pyruvate dehydrogenase complex from broccoli floral buds

1977

Rubin, P.M.; Randall, D.D.

Arch. Biochem. Biophys.

178

342-349

348974

956154

Properties and subunit structure of pig heart pyruvate dehydrogenase

1976

Hamada, M.; Hiraoka, T.; Koike, K.; Ogasahara, K.; Kanzaki, T.; Koike, M.

J. Biochem.

79

1273-1285

348976

1204621

The pyruvate-dehydrogenase complex from Azotobacter vinelandii

1975

Bresters, T.W.; de Abreu, R.A.; de Kok, A.; Visser, J.; Veeger, C.

Eur. J. Biochem.

59

335-345

348978

4342189

Isolation and properties of a pyruvate dehydrogenase complex from the yeast Hansenula miso

1972

Hirabayashi, T.; Harada, T.

J. Biochem.

71

797-804

348980

4317491

The pyruvate dehydrogenase complex from the mitochondrial fraction of Neurospora crassa

1970

Harding, R.W.; Caroline, D.F.; Wagner, R.P.

Arch. Biochem. Biophys.

138

653-661

348981

-

Purification and resolution of the pyruvate dehydrogenase complex (Escherichia coli)

1966

Reed, L.J.; Willms, C.R.

Methods Enzymol.

9

247-265

348982

6373436

Cloning and sequence analysis of the pyruvate and 2-oxoglutarate dehydrogenase complex genes of Escherichia coli

1984

Guest, J.R.; Darlison, M.G.; Spencer, M.E.; Stephens, P.E.

Biochem. Soc. Trans.

12

220-223

348997

2404759

The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component

1990

Schulze, E.; Westphal, A.H.; Hanemaaijer, R.; de Kok A.

Eur. J. Biochem.

187

229-234

348998

2500417

Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively

1989

Carlsson, P.; Hederstedt, L.

J. Bacteriol.

171

3667-3672

348999

2503710

Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase

1989

Repetto, B.; Tzagoloff, A.

Mol. Cell. Biol.

9

2695-2705

349000

-

alpha-Ketoglutarate dehydrogenase from cauliflower mitochondria: preparation and reactivity with substrates

1989

Karam, G.A.; Bishop, S.H.

Phytochemistry

28

3291-3293

349001

2597117

The binding of Ca2+ ions to pig heart NAD+-isocitrate dehydrogenase and the 2-oxoglutarate dehydrogenase complex

1989

Rutter, G.A.; Denton, R.M.

Biochem. J.

263

453-462

349002

2778429

Purification and characterization of the 2-oxoglutarate dehydrogenase complex from Dictyostelium discoideum

1989

Heckert, L.L.; Butler, M.H.; Reimers, J.M.; Albe, K.R.; Wright, B.E.

J. Gen. Microbiol.

135

155-161

349003

2521564

Neurospora crassa alpha-ketoglutarate dehydrogenase complex: description, resolution of components and catalytic properties

1989

Bessam, H.; Mareck, A.M.; Foucher, B.

Biochim. Biophys. Acta

990

66-72

349004

-

alpha-Ketoglutarate dehydrogenase complex from Escherichia coli

1969

Reed, L.J.; Mukherjee, B.B.

Methods Enzymol.

13

55-61

349005

-

alpha-Ketoglutarate dehydrogenase from pig heart

1969

Sanadi, D.R.

Methods Enzymol.

13

52-55

349006

3207422

Calcium sensitive isocitrate and 2-oxoglutarate dehydrogenase activities in rat liver and AS-30D hepatoma mitochondria

1988

Murphy, A.N.; Kelleher, J.K.; Fiskum, G.

Biochem. Biophys. Res. Commun.

157

1218-1255

349007

3416997

Transketolase and 2-oxoglutarate dehydrogenase activities in the brain and liver of the developing rat

1988

Iwata, H.; Tonomura, H.; Matsuda, T.

Experientia

44

780-781

349008

16666143

Haloxyfop inhibition of the pyruvate and the alpha-ketoglutarate dehydrogenase complexes of corn (Zea mays L.) and soybean (Glycine max [L.] Merr.)

1988

Cho, H.Y.; Widholm, J.M.; Slife, F.W.

Plant Physiol.

87

334-340

349009

3631965

2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: interaction via a common coenzyme a pool

1987

Dry, I.B.; Wiskich, J.T.

Arch. Biochem. Biophys.

257

92-99

349010

-

Isocitrate and oxoglutarate dehydrogenase activities of murine dystrophic skeletal muscle

1987

Burke, L.A.; Heffron, J.J.A.

Biochem. Soc. Trans.

15

233-234

349011

-

Precursor forms of the constituent polypeptides of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes from ox heart

1986

De Marcucci, O.G.L.; Hunter, A.; Lindsay, J.G.

Biochem. Soc. Trans.

14

870

349013

3948874

Immunological and biosynthetic studies on the mammalian 2-oxoglutarate dehydrogenase multienzyme complex

1986

Hunter, A.; Lindsay, J.G.

Eur. J. Biochem.

155

103-109

349014

2994628

Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate

1985

Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latipää, P.; Gunzler, V.; Hanauske-Abel, H.M.; Hassinen, I.E.; Kivirikko, K.I.

Biochem. J.

229

127-133

349015

3968029

Presence and regulation of the alpha-ketoglutarate dehydrogenase multienzyme complex in the filamentous fungus Aspergillus niger

1985

Meixner-Monori, B.; Kubicek, C.P.; Habison, A.; Kubicek-Pranz, E.M.; Roehr, M.

J. Bacteriol.

161

265-271

349017

-

Inhibition of bovine kidney alpha-ketoglutarate dehydrogenase complex by reduced nicotinamide adenine dinucleotide in the presence or absence of calcium ion and effect of adenosine 5'-diphosphate on reduced nicotinamide adenine dinucleotide inhibition

1981

Lawlis, V.B.; Roche, T.E.

Biochemistry

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2319-2324

349018

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Presence and regulation of alphe-ketoglutarate dehydrogenase complex in a glutamate-producing bacterium Brevibacterium flavum

1980

Shiio, I.; Ujigawa-Takeda, U.

Agric. Biol. Chem.

44

1897-1904

349019

6896181

Subunit composition and partial reactions of the 2-oxoglutarate dehydrogenase complex of Acetobacter xylinum

1980

De Kok, A.; Kornfeld, S.; Benziman, M.; Milner, Y.

Eur. J. Biochem.

106

49-58

349020

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Evidence for the identity and some comparative properties of alpha-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity

1980

Gupta, S.C.; Dekker, E.E.

J. Biol. Chem.

255

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349021

373631

Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli alpha-ketoglutarate dehydrogenase complex

1979

Gupta, S.C.; Dekker, E.E.

Arch. Biochem. Biophys.

192

324-326

349022

6380583

Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation

1984

Waskiewicz, D.E.; Hammes, G.G.

Biochemistry

23

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349023

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Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart

1977

McMinn, C.L.; Ottaway, J.H.

Biochem. J.

161

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349024

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alpha-Ketoglutarate dehydrogenase complex of Acetobacter xylinum. Purification and regulatory properties

1977

Kornfeld, S.; Benziman, M.; Milner, Y.

J. Biol. Chem.

252

2940-2947

349025

4359921

The purification and regulatory properties of alpha-oxoglutarate dehydrogenase from Acinetobacter lwoffi

1973

Parker, M.G.; Weitzman, P.D.J.

Biochem. J.

135

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349026

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Mammalian alpha-keto acid dehydrogenase complexes. II. An improved procedure for the preparation of 2-oxoglutarate dehydrogenase complex from pig heart muscle

1967

Hirashima, M.; Hayakawa, T.; Koike, M.

J. Biol. Chem.

242

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349027

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Mammalian alpha-keto acid dehydrogenase complexes. IV. Substrate specificities and kinetic properties of the pig heart pyruvate and 2-oxoglutarate dehydrogenase complexes

1969

Kanzaki, T.; Hayakawa, T.; Hamada, M.; Fukuyoshi, Y.; Koike, M.

J. Biol. Chem.

244

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349028

4338236

Mammalian alpha-keto acid dehydrogenase complexes. VII. Resolution and reconstitution of the pig heart 2-oxoglutarate dehydrogenase complex

1972

Tanaka, N.; Koike, K.; Hamada, M.; Otsuka, K.; Suematsu, T.; Koike, M.

J. Biol. Chem.

247

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349029

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alpha-Keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex

1973

Pettit, F.H.; Hamilton, L.; Munk, P.; Namihira, G.; Eley, M.H.; Willms, C.R.; Reed, L.J.

J. Biol. Chem.

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349030

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Inhibition of the alpha-ketoglutarate dehydrogenase complex from baker's yeast by acetaldehyde and glyoxylate

1972

Hirabayashi, T.; Harada, T.

Agric. Biol. Chem.

36

1249-1251

349031

11946628

Regulation of alpha-ketoglutarate dehydrogenase activity in Acinetobacter

1972

Weitzman, P.D.J.

FEBS Lett.

22

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349032

4942727

Isolation and properties of alpha-ketoglutarate dehydrogenase complex from bakers yeast (Saccharomyces cerevisiae)

1971

Hirabayashi, T.; Harada, T.

Biochem. Biophys. Res. Commun.

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1369-1375

349033

10788456

Zn2+ inhibits alpha-ketoglutarate-stimulated mitochondrial respiration and the isolated alpha-ketoglutarate dehydrogenase complex

2000

Brown, A.M.; Kristal, B.S.; Effron, M.S.; Shestopalov, A.I.; Ullucci, P.A.; Sheu, K.F.; Blass, J.P.; Cooper, A.J.

J. Biol. Chem.

275

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349034

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Oxidative metabolites of 5-S-cysteinyldopamine inhibit the alpha-ketoglutarate dehydrogenase complex: possible relevance to the pathogenesis of Parkinson's disease

2000

Shen, X.M.; Li, H.; Dryhurst, G.

J. Neural Transm.

107

959-978

349035

10956063

Oxidative metabolites of 5-S-cysteinylnorepinephrine are irreversible inhibitors of mitochondrial complex I and the alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase complexes: possible implications for neurodegenerative brain disorders

2000

Xin, W.; Shen, X.M.; Li, H.; Dryhurst, G.

Chem. Res. Toxicol.

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349036

7662887

Inhibition of alpha-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

1995

McNaught, K.S.; Altomare, C.; Cellamare, S.; Carotti, A.; Thull, U.; Carrupt, P.A.; Testa, B.; Jenner, P.; Marsden, C.D.

NeuroReport

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1105-1108

349037

8474555

The two catalytic components of the 2-oxoglutarate dehydrogenase complex in rat cerebral synaptic and nonsynaptic mitochondria: Comparison of the response to in vitro treatment with ammonia, hyperammonemia, and hepatic encephalopathy

1993

Faff-Michalak, L.; Albrecht, J.

Neurochem. Res.

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349038

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The alpha-ketoglutarate dehydrogenase complex in neurodegeneration

2000

Gibson, G.E.; Park, L.C.H.; Sheu, K.F.R.; Blass, J.P.; Calingasan, N.Y.

Neurochem. Int.

36

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349039

8867378

Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex

1996

Hein, S.; Steinbuechel, A.

FEMS Microbiol. Lett.

136

231-238

349040

10745006

Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease

2000

Aevarsson, A.; Chuang, J.L.; Wynn, R.M.; Turley, S.; Chuang, D.T.; Hol, W.G.J.

Structure

8

277-291

349041

7980405

Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD+-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart

1994

Nichols, B.J.; Rigoulet, M.; Denton, R.M.

Biochem. J.

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349042

10672230

The alpha-ketoglutarate dehydrogenase complex

1999

Sheu, K.F.R.; Blass, J.P.

Ann. N. Y. Acad. Sci.

893

61-78

349043

8612743

Succinyl phosphonate inhibits alpha-ketoglutarate oxidative decarboxylation, catalyzed by alpha-ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle

1996

Biryukov, A.I.; Bunik, V.I.; Zhukov, Y.N.; Khurs, E.N.; Khomutov, R.M.

FEBS Lett.

382

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349044

10848975

Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate

2000

Bunik, V.; Westphal, A.H.; de Kok, A.

Eur. J. Biochem.

267

3583-3591

349045

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Branched-chain ketoacid dehydrogenase

1987

Randle, P.J.; Patston, P.A.; Espinal, J.

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

18

97-121

392950

3136140

The novel disulfide reductase bis-gamma-glutamylcystine reductase and dihydrolipoamide dehydrogenase from Halobacterium halobium: Purification by immobilized-metal-ion affinity chromatography and properties of the enzymes

1988

Sundquist, A.R.; Fahey, R.C.

J. Bacteriol.

170

3459-3467

393962

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Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi

1990

Lohrer, H.; Krauth-Siegel, R.L.

Eur. J. Biochem.

194

863-869

393964

2294086

Purification and comparative studies of dihydrolipoamide dehydrogenases from the anaerobic, glycine-utilizing bacteria Peptostreptococcus glycinophilus, Clostridium cylindrosporum, and Clostridium sporogenes

1990

Dietrichs, D.; Andreesen, J.R.

J. Bacteriol.

172

243-251

394002

11788775

Molecular cloning, functional characterization, and subcellular localization of soybean nodule dihydrolipoamide reductase

2002

Moran, J.F.; Sun, Z.; Sarath, G.; Arredondo-Peter, R.; James, E.K.; Becana, M.; Klucas, R.V.

Plant Physiol.

128

300-313

394004

10336857

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

1999

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

Protein Expr. Purif.

16

27-39

394006

11560483

Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes

2001

Argyrou, A.; Blanchard, J.S.

Biochemistry

40

11353-11363

394007

9143318

Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis

1997

Marcinkeviciene, J.; Blanchard, J.S.

Arch. Biochem. Biophys.

340

168-176

394009

9858775

Lipoamide dehydrogenase from Streptomyces seoulensis: biochemical and genetic properties

1998

Youn, H.; Kwak, J.; Youn, H.D.; Hah, Y.C.; Kang, S.O.

Biochim. Biophys. Acta

1388

405-418

394011

10806385

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system

2000

Neuburger, M.; Polidori, A.M.; Pietre, E.; Faure, M.; Jourdain, A.; Bourguignon, J.; Pucci, B.; Douce, R.

Eur. J. Biochem.

267

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394513

12232320

Overproduction in Escherichia coli and characterization of a soybean ferric leghemoglobin reductase

1994

Ji, L.; Becana, M.; Sarath, G.; Shearman, L.; Klucas, R.V.

Plant Physiol.

106

203-209

486168

1898934

Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system

1991

Oppermann, F.B.; Schmidt, B.; Steinbuchel, A.

J. Bacteriol.

173

757-767

656835

15612914

The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases

2005

McMillan, P.J.; Stimmler, L.M.; Foth, B.J.; McFadden, G.I.; Mueller, S.

Mol. Microbiol.

55

27-38

658799

12688423

Phenothiazine radicals inactivate Trypanosoma cruzi dihydrolipoamide dehydrogenase: enzyme protection by radical scavengers

2003

Gutierrez-Correa, J.; Krauth-Siegel, R.L.; Stoppani, A.O.

Free Radic. Res.

37

281-291

659167

11744691

Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase

2002

Gazaryan, I.G.; Krasnikov, B.F.; Ashby, G.A.; Thorneley, R.N.; Kristal, B.S.; Brown, A.M.

J. Biol. Chem.

277

10064-10072

667913

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Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes

2006

Brownlee, J.M.; Carlson, E.; Milne, A.C.; Pape, E.; Harrison, D.H.

Bioorg. Chem.

34

424-444

673190

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Trypanosoma cruzi dihydrolipoamide dehydrogenase as target for phenothiazine cationic radicals. Effect of antioxidants

2006

Gutierrez-Correa, J.

Curr. Drug Targets

7

1155-1179

673411

17158739

Proteins of the glycine decarboxylase complex in the hydrogenosome of Trichomonas vaginalis

2006

Mukherjee, M.; Brown, M.T.; McArthur, A.G.; Johnson, P.J.

Eukaryot. Cell

5

2062-2071

674943

17171578

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

2007

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

J. Biomed. Sci.

14

203-210

684365

18032470

O2 uptake kinetics, pyruvate dehydrogenase activity, and muscle deoxygenation in young and older adults during the transition to moderate-intensity exercise

2008

Gurd, B.J.; Peters, S.J.; Heigenhauser, G.J.; LeBlanc, P.J.; Doherty, T.J.; Paterson, D.H.; Kowalchuk, J.M.

Am. J. Physiol. Regul. Integr. Comp. Physiol.

294

R577-R584

685585

17644334

Theoretical calculation of the binding free energies for pyruvate dehydrogenase E1 binding with ligands

2007

Xiong, Y.; Li, Y.; He, H.; Zhan, C.G.

Bioorg. Med. Chem. Lett.

17

5186-5190

686469

17449654

Carbohydrate metabolism in the Toxoplasma gondii apicoplast: localization of three glycolytic isoenzymes, the single pyruvate dehydrogenase complex, and a plastid phosphate translocator

2007

Fleige, T.; Fischer, K.; Ferguson, D.J.; Gross, U.; Bohne, W.

Eukaryot. Cell

6

984-996

687812

18180296

Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases

2008

Gey, U.; Czupalla, C.; Hoflack, B.; Roedel, G.; Krause-Buchholz, U.

J. Biol. Chem.

283

9759-9767

691392

18391450

Characterization of a dihydrolipoyl dehydrogenase having diaphorase activity of Clostridium kluyveri

2008

Chakraborty, S.; Sakka, M.; Kimura, T.; Sakka, K.

Biosci. Biotechnol. Biochem.

72

982-988

692385

18312361

The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens

2008

Batista, A.P.; Kletzin, A.; Pereira, M.M.

FEMS Microbiol. Lett.

281

147-154

692858

18375566

Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12

2008

Kim, Y.; Ingram, L.O.; Shanmugam, K.T.

J. Bacteriol.

190

3851-3858

693005

17690105

Enzymatic characterization of dihydrolipoamide dehydrogenase from Streptococcus pneumoniae harboring its own substrate

2007

Hakansson, A.P.; Smith, A.W.

J. Biol. Chem.

282

29521-29530

694854

17404228

Cryptic proteolytic activity of dihydrolipoamide dehydrogenase

2007

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

Proc. Natl. Acad. Sci. USA

104

6158-6163

698965

19054767

Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1

2009

Cheng, Q.; Sandalova, T.; Lindqvist, Y.; Arner, E.S.

J. Biol. Chem.

284

3998-4008

699660

19393031

Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid

2009

Ambrus, A.; Tretter, L.; Adam-Vizi, V.

J. Neurochem.

109 Suppl 1

222-229

711320

19383527

Moonlighting protein in Starkeyomyces koorchalomoides: characterization of dihydrolipoamide dehydrogenase as a protein acetyltransferase utilizing acetoxycoumarin as the acetyl group donor

2009

Tyagi, T.K.; Ponnan, P.; Singh, P.; Bansal, S.; Batra, A.; Collin, F.; Guillonneau, F.; Jore, D.; Patkar, S.A.; Saxena, R.K.; Parmar, V.S.; Rastogi, R.C.; Raj, H.G.

Biochimie

91

868-875

712521

20159566

Gene cloning and characterization of dihydrolipoamide dehydrogenase from Microbacterium luteolum: A useful enzymatic regeneration system of NAD+ from NADH

2010

Kurokawa, J.; Asano, M.; Nomoto, S.; Makino, Y.; Itoh, N.

J. Biosci. Bioeng.

109

218-223

713314

20488895

Disruption of ptLPD1 or ptLPD2, genes that encode isoforms of the plastidial lipoamide dehydrogenase, confers arsenate hypersensitivity in Arabidopsis

2010

Chen, W.; Chi, Y.; Taylor, N.L.; Lambers, H.; Finnegan, P.M.

Plant Physiol.

153

1385-1397

713453

19481152

A novel protein that binds to dnrN-dnrO intergenic region of Streptomyces peucetius purified by DNA affinity capture has dihydrolipoamide dehydrogenase activity

2009

Ajith, V.K.; Prasad, R.

Protein Expr. Purif.

67

132-138

713461

20093189

Cloning and purification of recombinant silkworm dihydrolipoamide dehydrogenase expressed in Escherichia coli

2010

Huo, J.; Shi, H.; Yao, Q.; Chen, H.; Wang, L.; Chen, K.

Protein Expr. Purif.

72

95-100

724002

20833784

Dihydrolipoamide dehydrogenases of Advenella mimigardefordensis and Ralstonia eutropha catalyze cleavage of 3,3-dithiodipropionic acid into 3-mercaptopropionic acid

2010

Wuebbeler, J.H.; Raberg, M.; Brandt, U.; Steinbuechel, A.

Appl. Environ. Microbiol.

76

7023-7028

725059

21172426

Substrate and inhibitor specificities differ between human cytosolic and mitochondrial thioredoxin reductases: Implications for development of specific inhibitors

2011

Rackham, O.; Shearwood, A.M.; Thyer, R.; McNamara, E.; Davies, S.M.; Callus, B.A.; Miranda-Vizuete, A.; Berners-Price, S.J.; Cheng, Q.; Arner, E.S.; Filipovska, A.

Free Radic. Biol. Med.

50

689-699

742126

25387830

Biochemical and structural characterization of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparum

2015

Laine, L.M.; Biddau, M.; Byron, O.; Mueller, S.

Biosci. Rep.

35

e00171

742565

27178006

Functional thioredoxin reductase from pathogenic and free-living Leptospira spp.

2016

Sasoni, N.; Iglesias, A.A.; Guerrero, S.A.; Arias, D.G.

Free Radic. Biol. Med.

97

1-13

754090

20463026

Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase

2010

Cussiol, J.R.; Alegria, T.G.; Szweda, L.I.; Netto, L.E.

J. Biol. Chem.

285

21943-21950

Links to other databases for Lipoamide

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