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Ligand lipoamide

Basic Ligand Information

Molecular Structure

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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 (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH

-

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH + H+

-

-

1.8.1.4

2 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 (10 results)

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Show Product (10 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

-

-

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

3 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

20

2319-2324

349018

-

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

6985904

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

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

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

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Branched-chain ketoacid dehydrogenase

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

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392950

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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

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Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi

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

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

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

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

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

2001

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Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis

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Lipoamide dehydrogenase from Streptomyces seoulensis: biochemical and genetic properties

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

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

2000

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

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

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The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases

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

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

2002

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673411

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

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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.

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

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

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

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Characterization of a dihydrolipoyl dehydrogenase having diaphorase activity of Clostridium kluyveri

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692385

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The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens

2008

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

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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.

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

2007

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

J. Biol. Chem.

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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

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Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1

2009

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

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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

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712521

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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.

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

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

Plant Physiol.

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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

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713461

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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.

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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.

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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.

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

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

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

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

Free Radic. Biol. Med.

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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.

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