print visible entries

print all entries

Ligand dihydrolipoamide

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

top print hide

Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH

659101, 659482, 656835

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH + H+

741757, 742126, 743127, 743008, 741807, 741998, 742087, 742221, 743050, 743051, 743052, 742909, 743450

-

1.8.1.4

2 entries

2.3.1.12

dihydrolipoamide + acetyl-CoA = S-acetyldihydrolipoamide + CoA

348948, 94881, 348910, 348964, 486184, 486239, 348932, 348946, 348961, 348967, 348982, 486166, 486181, 486186, 486192, 486198, 486199, 486201, 486204, 486206, 486207, 486208, 486209, 486210, 486236, 486237, 486179, 486229, 486231, 486240, 348941, 486180, 486202, 348959, 486169, 94893, 348927, 348938, 348955, 486174, 486175, 486176, 486194, 486195, 486196, 486197, 486235, 348965, 393963, 486167, 486178, 486225, 486226, 486230, 348954, 486232, 486227, 486233, 486224, 486170, 486171, 486172, 486173, 486177, 486185, 486217, 486228, 486216, 348951, 348950, 348949, 486168, 486238, 486203

-

2.3.1.61

succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide

487347, 487348, 348914, 349029, 487333, 487337, 487339, 487340, 487345, 487346, 487341, 487344, 487343, 487349, 349039, 349019, 487335, 487336

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.4

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

0

-

1.8.1.4

lipoamide + NADH + H+ = dihydrolipoamide + NAD+

0

-

1.8.1.4

2 entries

Substrate in Enzyme-catalyzed Reactions (22 results)

top print hide

Show Substrate (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.28

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

758317

-

1.11.1.28

H2O2 + dihydrolipoamide = H2O + lipoamide

758317

-

1.11.1.28

linoleic acid hydroperoxide + dihydrolipoamide = ? + lipoamide

758317

-

1.11.1.28

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

758317

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH

348948, 393971, 393995, 348944, 393968, 393993, 393999, 348981, 393966, 393987, 393988, 393992, 393994, 394003, 394004, 659101, 711099, 349067, 393986, 691036, 693975, 393969, 393982, 393996, 394000, 712097, 393970, 393975, 393984, 394007, 393963, 394001, 394011, 394012, 393973, 349054, 393980, 393965, 392950, 393978, 393981, 394005, 693005, 393991, 393998, 394006, 659482, 393964, 348939, 393962, 393976, 712087, 656835, 394008, 393990, 486168, 394009, 394002, 691392, 713461, 693271, 394010, 727213, 727409, 727729, 711225, 393989, 393974, 692385

-

1.8.1.4

dihydrolipoamide + NAD+ = lipoamide + NADH + H+

672465, 672869, 673943, 674382, 674759, 675350, 677161, 691569, 724686, 764703, 741757, 673517, 674368, 764862, 764880, 673190, 742126, 743127, 674430, 743008, 674479, 674943, 763920, 765207, 765208, 765209, 765210, 765736, 741807, 741998, 742087, 742221, 743050, 743051, 743052, 742909, 743450

-

1.8.1.4

dihydrolipoamide + NADP+ = lipoamide + NADPH

393964

-

1.8.1.4

DL-6,8-thiooctic acid amide + NADH = ? + NAD+

659167

-

1.8.1.4

reduced DL-lipoamide + NAD+ = oxidized DL-lipoamide + NADH

657980

-

1.11.1.28

4 entries

1.8.1.4

5 entries

1.8.4.2

dihydrolipoamide + protein disulfide = ?

394815

-

2.3.1.12

dihydrolipoamide + acetyl-CoA = S-acetyldihydrolipoamide + CoA

348948, 94881, 348910, 348964, 486184, 486239, 348932, 348946, 348961, 348967, 348982, 486166, 486181, 486186, 486192, 486198, 486199, 486201, 486204, 486206, 486207, 486208, 486209, 486210, 486236, 486237, 486179, 486229, 486231, 486240, 348941, 486180, 486202, 348959, 486169, 94893, 348927, 348938, 348955, 486174, 486175, 486176, 486194, 486195, 486196, 486197, 486235, 486203, 348965, 393963, 486167, 486178, 486225, 486226, 486230, 348954, 486232, 486227, 486233, 486224, 486170, 486171, 486172, 486173, 486177, 486185, 486217, 486228, 486216, 348951, 348950, 348949, 486168, 486238

-

2.3.1.168

2-methylpropanoyl-CoA + dihydrolipoamide = CoA + S-2-methylpropanoyldihydrolipoamide

644839

-

2.3.1.168

2-oxoglutaryl-CoA + dihydrolipoamide = CoA + S-(2-oxoglutaryl)dihydrolipoamide

644848

-

2.3.1.168

3-methylisovaleryl-CoA + dihydrolipoamide = CoA + S-(3-methylisovaleryl)dihydrolipoamide

644848

-

2.3.1.168

4-methylthiobutyryl-CoA + dihydrolipoamide = CoA + S-(4-methylthiobutyryl)dihydrolipoamide

644848

-

2.3.1.168

acetyl-CoA + dihydrolipoamide = CoA + S-acetyldihydrolipoamide

644839, 644846

-

2.3.1.168

butyryl-CoA + dihydrolipoamide = CoA + S-butyryldihydrolipoamide

644848

-

2.3.1.168

isobutyryl-CoA + dihydrolipoamide = CoA + S-isobutyryldihydrolipoamide

644839

-

2.3.1.168

isocaproyl-CoA + dihydrolipoamide = CoA + S-isohexanoyldihydrolipoamide

644848

-

2.3.1.168

isovaleryl-CoA + dihydrolipoamide = CoA + S-isovaleryldihydrolipoamide

644839, 644848, 644842

-

2.3.1.61

succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide

487347, 487348, 348914, 349029, 487333, 487337, 487339, 487340, 487345, 487346, 487341, 487344, 487336, 487343, 487349, 349039, 349019, 487335

-

2.3.1.61

succinyl-CoA + DL-dihydrolipoamide = CoA + S-succinyldihydrolipoamide

755867

-

2.3.1.168

9 entries

2.3.1.61

2 entries

Product in Enzyme-catalyzed Reactions (12 results)

top print hide

Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.4

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

0

-

1.8.1.4

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

0

-

1.8.1.4

alpha-lipoamide + NADH = dihydrolipoamide + NAD+

0

-

1.8.1.4

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

0

-

1.8.1.4

lipoamide + 3-acetylpyridine adenine dinucleotide = dihydrolipoamide + ?

0

-

1.8.1.4

lipoamide + NADH + H+ = dihydrolipoamide + NAD+

0

-

1.8.1.4

lipoamide + NADH = dihydrolipoamide + NAD+

0

-

1.8.1.4

lipoamide + nicotinamide hypoxanthine dinucleotide = dihydrolipoamide + ?

0

-

1.8.1.4

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

0

-

1.8.1.4

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

0

-

1.8.1.4

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

0

-

1.8.1.4

11 entries

1.8.1.9

lipoamide + NADPH + H+ = dihydrolipoamide + NADP+

0

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.21

binds very tight to the enzyme, best inhibitor of the investigated, competitive

667913

-

1.8.1.4

-

727409

-

3.1.3.43

-

94880

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (45 results)

top print hide

Show Turnover Number (45 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.8.1.4

0.012

-

enzyme variant 2, at pH 7.5 and 37°C

764862

1.8.1.4

0.122

-

enzyme variant 1, at pH 7.5 and 37°C

764862

1.8.1.4

0.42

-

enzyme mutant C50A, pH 8.0, 37°C

743051

1.8.1.4

0.46

-

enzyme mutant C50T, pH 8.0, 37°C

743051

1.8.1.4

6

-

mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA

724686

1.8.1.4

8.5

-

mutant enzyme S53K/K54S

394004

1.8.1.4

16.2

-

mutant enzyme L99A, at pH 8.0 and 37°C

765208

1.8.1.4

29.7

-

mutant enzyme E192Q

394004

1.8.1.4

37

-

enzyme mutant H329A, pH 8.0, 37°C

743052

1.8.1.4

107

-

mutant D320N

674943

1.8.1.4

107

-

mutant enzyme D320N

674943

1.8.1.4

110

-

pH 8.0, 25°C, recombinant His-tagged enzyme

742126

1.8.1.4

116

-

mutant enzyme N286Q

674943

1.8.1.4

116

-

mutant enzyme P387A, at pH 8.0 and 37°C

765210

1.8.1.4

116

-

mutant N286Q

674943

1.8.1.4

159

-

mutant enzyme N286D

674943

1.8.1.4

159

-

mutant N286D

674943

1.8.1.4

220

-

mutant R281N

693271

1.8.1.4

223

-

mutant R281K

693271

1.8.1.4

448

-

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

656835

1.8.1.4

505

-

wild type enzyme

674943

1.8.1.4

505

-

wild-type

674943

1.8.1.4

505

-

wild-type E3

693271

1.8.1.4

567

-

wild-type enzyme

394004

1.8.1.4

624

-

mutant enzyme P355A, at pH 8.0 and 37°C

765209

1.8.1.4

629

-

enzyme mutant P303A, pH 8.0, 37°C

743050

1.8.1.4

655

-

mutant T148G

693271

1.8.1.4

711

-

mutant enzyme P423A, at pH 8.0 and 37°C

765207

1.8.1.4

742

-

mutant T148S

693271

1.8.1.4

817

-

enzyme mutant P156A, pH 8.0, 37°C

743050

1.8.1.4

899

-

wild type enzyme, at pH 8.0 and 37°C

765207, 765208, 765209, 765210

1.8.1.4

899

-

wild-type enzyme, pH 8.0, 37°C

743050, 743051, 743052

1.8.1.4

899

-

wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA

724686

1.8.1.4

1032

-

mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA

724686

1.8.1.4

1309

-

mutant enzyme P154A, at pH 8.0 and 37°C

765207

2.3.1.61

3

-

mutant enzyme D423G, at pH 8.0 and 30°C

755867

2.3.1.61

3

-

mutant enzyme H419G, at pH 8.0 and 30°C

755867

2.3.1.61

6

-

mutant enzyme H419D, at pH 8.0 and 30°C

755867

2.3.1.61

7

-

mutant enzyme D423A, at pH 8.0 and 30°C

755867

2.3.1.61

7

-

mutant enzyme D423DEL, at pH 8.0 and 30°C

755867

2.3.1.61

7

-

mutant enzyme H419A, at pH 8.0 and 30°C

755867

2.3.1.61

11

-

mutant enzyme H419S, at pH 8.0 and 30°C

755867

2.3.1.61

18

-

mutant enzyme D423S, at pH 8.0 and 30°C

755867

2.3.1.61

165

-

mutant enzyme D423E, at pH 8.0 and 30°C

755867

2.3.1.61

186

-

wild type enzyme, at pH 8.0 and 30°C

755867

1.8.1.4

35 entries

2.3.1.61

10 entries

K_M Value (95 results)

top print hide

Show KM Value (95 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.1.4

0.0107

-

pH 7.0, 30°C, mutant enzyme E423A

727409

1.8.1.4

0.0157

-

pH 7.0, 30°C, mutant enzyme E423D, assay in the absence of KCI

727409

1.8.1.4

0.017

-

-

393981

1.8.1.4

0.0177

-

pH 7.0, 30°C, mutant enzyme E423Q, assay in the absence of KCI

727409

1.8.1.4

0.018

-

pH 8.0, 37°C

727729

1.8.1.4

0.0228

-

pH 7.0, 30°C, mutant enzyme E423Q

727409

1.8.1.4

0.023

-

pH 7.0, 30°C, mutant enzyme E423S

727409

1.8.1.4

0.0243

-

pH 7.0, 30°C, mutant enzyme E423A, assay in the absence of KCI

727409

1.8.1.4

0.025

-

-

393966

1.8.1.4

0.0266

-

pH 7.0, 30°C, mutant enzyme E423D

727409

1.8.1.4

0.0269

-

pH 7.0, 30°C, wild-type enzyme

727409

1.8.1.4

0.027

-

enzyme mutant, pH 8.0, 37°C

742221

1.8.1.4

0.0274

-

pH 7.0, 30°C, wild-type enzyme, assay in the absence of KCI

727409

1.8.1.4

0.031

-

mutant enzyme P387A, at pH 8.0 and 37°C

765210

1.8.1.4

0.0364

-

pH 7.0, 30°C, mutant enzyme E423S, assay in the absence of KCI

727409

1.8.1.4

0.04

-

recombinant DLDH expressed without without a lipoyl protein domain

693005

1.8.1.4

0.046

-

37°C, pH 8.0

727213

1.8.1.4

0.05

-

mutant enzyme S53K/K54S

394004

1.8.1.4

0.056

-

recombinant DLDH

693005

1.8.1.4

0.064

-

recombinant DLDH expressed without lipoic acid

693005

1.8.1.4

0.08

-

complex-bound dihydrolipoamide dehydrogenase

393988

1.8.1.4

0.09

-

mutant P325A, pH 8.0, 37°C, presence of 1.5 mM EDTA

724686

1.8.1.4

0.12

-

mutant enzyme E192Q

394004

1.8.1.4

0.12

-

mutant R281K

693271

1.8.1.4

0.13

-

-

393976

1.8.1.4

0.146

-

pH 8.0, 25°C, mitochondrial isozyme

656835

1.8.1.4

0.16

-

enzyme mutant C50T, pH 8.0, 37°C

743051

1.8.1.4

0.16

-

enzyme mutant H329A, pH 8.0, 37°C

743052

1.8.1.4

0.19

-

wild-type enzyme, pH 8.0, 37°C

743052

1.8.1.4

0.2

-

mutant enzyme N286Q

674943

1.8.1.4

0.2

-

mutant N286Q

674943

1.8.1.4

0.22

-

enzyme mutant C50A, pH 8.0, 37°C

743051

1.8.1.4

0.28

-

free dihydrolipoamide dehydrogenase

393988

1.8.1.4

0.3

-

-

691392

1.8.1.4

0.31

-

mutant enzyme L99A, at pH 8.0 and 37°C

765208

1.8.1.4

0.38

-

mutant R281N

693271

1.8.1.4

0.38

-

wild type enzyme

674943

1.8.1.4

0.38

-

wild-type

674943

1.8.1.4

0.38

-

wild-type E3

693271

1.8.1.4

0.4

-

-

486168

1.8.1.4

0.48

-

-

393984

1.8.1.4

0.52

-

mutant enzyme P355A, at pH 8.0 and 37°C

765209

1.8.1.4

0.55

-

enzyme mutant P303A, pH 8.0, 37°C

743050

1.8.1.4

0.58

-

mutant T148G

693271

1.8.1.4

0.58

-

mutant W366A, pH 8.0, 37°C, presence of 1.5 mM EDTA

724686

1.8.1.4

0.59

-

mutant T148S

693271

1.8.1.4

0.63

-

enzyme mutant P156A, pH 8.0, 37°C

743050

1.8.1.4

0.63

-

wild-type enzyme, pH 8.0, 37°C

742221

1.8.1.4

0.64

-

wild type enzyme, at pH 8.0 and 37°C

765207, 765208, 765209, 765210

1.8.1.4

0.64

-

wild-type enzyme, pH 8.0, 37°C

743050, 743051

1.8.1.4

0.64

-

wild-type, pH 8.0, 37°C, presence of 1.5 mM EDTA

724686

1.8.1.4

0.69

-

native enzyme

394003

1.8.1.4

0.7

-

-

692385

1.8.1.4

0.7

-

mutant enzyme N286D

674943

1.8.1.4

0.7

-

mutant enzyme P423A, at pH 8.0 and 37°C

765207

1.8.1.4

0.7

-

mutant N286D

674943

1.8.1.4

0.76

-

mutant enzyme K37E

394003

1.8.1.4

0.8299

-

enzyme variant 2, at pH 7.5 and 37°C

764862

1.8.1.4

0.83

-

-

393974

1.8.1.4

0.87

-

mutant enzyme P154A, at pH 8.0 and 37°C

765207

1.8.1.4

0.88

-

wild-type enzyme

394004

1.8.1.4

1.15

-

mutant enzyme A48I, at pH 7.5 and 37°C

764880

1.8.1.4

1.16

-

pH 8.0, 25°C, recombinant His-tagged enzyme

742126

1.8.1.4

1.21

-

mutant D320N

674943

1.8.1.4

1.21

-

mutant enzyme D320N

674943

1.8.1.4

2.2

-

mutant enzyme D49G, at pH 7.5 and 37°C

764880

1.8.1.4

2.7

-

enzyme variant 1, at pH 7.5 and 37°C

764862

1.8.1.4

2.9

-

mutant enzyme H457Q

394003

1.8.1.4

3.56

-

wild type enzyme, at pH 7.5 and 37°C

764880

1.8.1.4

3.9

-

mutant enzyme C38G, at pH 7.5 and 37°C

764880

1.8.1.4

4.7

-

mutant enzyme A54I, at pH 7.5 and 37°C

764880

1.8.1.4

18.4

-

mutant enzyme C15T, at pH 7.5 and 37°C

764880

1.8.1.4

43.6

-

mutant enzyme H452Q

394003

1.8.1.4

73 entries

1.8.4.2

0.14

-

-

394815

2.3.1.12

0.13

0.4

-

486203

2.3.1.12

1.08

-

N614D mutant

486228

2.3.1.12

1.2

-

catalytic domain after expression in Escherichia coli

486225

2.3.1.12

2.2

-

-

486168

2.3.1.12

4.2

-

-

486204

2.3.1.12

5.3

-

H610C mutant

486228

2.3.1.12

5.37

-

wild-type enzyme

486228

2.3.1.12

6.4

-

S558A mutant

486228

2.3.1.12

8 entries

2.3.1.168

2

-

pH 7.4, 37°C

644839

2.3.1.61

0.024

-

mutant enzyme H419S, at pH 8.0 and 30°C

755867

2.3.1.61

0.025

-

mutant enzyme H419DEL, at pH 8.0 and 30°C

755867

2.3.1.61

0.026

-

mutant enzyme H419A, at pH 8.0 and 30°C

755867

2.3.1.61

0.026

-

mutant enzyme H419G, at pH 8.0 and 30°C

755867

2.3.1.61

0.0274

-

wild type enzyme, at pH 8.0 and 30°C

755867

2.3.1.61

0.03

-

mutant enzyme H419D, at pH 8.0 and 30°C

755867

2.3.1.61

0.043

-

mutant enzyme D423S, at pH 8.0 and 30°C

755867

2.3.1.61

0.052

-

mutant enzyme D423G, at pH 8.0 and 30°C

755867

2.3.1.61

0.062

-

mutant enzyme D423A, at pH 8.0 and 30°C

755867

2.3.1.61

0.062

-

mutant enzyme D423DEL, at pH 8.0 and 30°C

755867

2.3.1.61

0.09

-

mutant enzyme D423E, at pH 8.0 and 30°C

755867

2.3.1.61

4.2

-

-

487348

2.3.1.61

12 entries

K_i Value (1 result)

top print hide

Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.1.4

0.023

-

pH 7.0, 30°C

727409

References & Links

Literature References (206)

top print hide

Show Reference (206 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

94880

2836411

Component requirements for NADH inhibition and spermine stimulation of pyruvate dehydrogenase phosphatase activity

1988

Rahmatullah, M.; Roche, T.E.

J. Biol. Chem.

263

8106-8110

94881

-

Pyruvate dehydrogenase

1987

Reed, L.J.; Yeaman, S.J.

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

18

77-95

94893

4401694

alpha-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart

1972

Linn, T.C.; Pelley, J.W.; Pettit, F.H.; Hucho, F.; Randall, D.D.; Reed, L.J.

Arch. Biochem. Biophys.

148

327-342

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

348927

-

Mammalian pyruvate dehydrogenase complex binds tightly to the mitochondrial inner membrane

1986

Phelps, A.; Lindsay, J.G.

Biochem. Soc. Trans.

14

893

348932

3899642

Hybrid pyruvate dehydrogenase complexes reconstituted from components of the complexes from Escherichia coli and Azotobacter vinelandii

1985

De Kok, A.; Westphal, A.H.

Eur. J. Biochem.

152

35-41

348938

6546521

Subunit binding in the pyruvate dehydrogenase complex from bovine kidney and heart

1984

Wu, T.L.; Reed, L.J.

Biochemistry

23

221-226

348939

6468378

The composition of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Does a unifying model exist for the complexes from gram-negative bacteria?

1984

Bosma, H.J.; de Kok, A.; Westphal, A.H.; Veeger, C.

Eur. J. Biochem.

142

541-549

348941

6412756

Purification and immunochemical studies of pyruvate dehydrogenase complex from rat heart, and cell-free synthesis of lipoamide dehydrogenase, a component of the complex

1983

Matuda, S.; Shirahama, T.; Saheki, T.; Miura, S.; Mori, M.

Biochim. Biophys. Acta

741

86-93

348944

6409095

Wild-type and mutant forms of the pyruvate dehydrogenase multienzyme complex from Bacillus subtilis

1983

Hodgson, J.A.; Lowe, P.N.; Perham, R.N.

Biochem. J.

211

463-472

348946

7041975

Reassociation of the pyruvate dehydrogenase complex from Escherichia coli: Kinetic measurements and binding studies by resonance energy transfer

1982

Graupe, K.; Abusaud, M.; Karfunkel, H.; Bisswanger, H.

Biochemistry

21

1386-1394

348948

7052136

Purification and properties of the pyruvate dehydrogenase complex from Salmonella typhimurium and formation of hybrids with the enzyme complex from Escherichia coli

1982

Seckler, R.; Binder, R.; Bisswanger, H.

Biochim. Biophys. Acta

705

210-217

348949

7144582

Pyruvate dehydrogenase complex from Hansenula

1982

Harada, T.; Hirabayashi, T.

Methods Enzymol.

89

420-423

348950

7144581

Pyruvate dehydrogenase complex from pigeon breast muscle

1982

Furuta, S.; Hashimoto, T.

Methods Enzymol.

89

414-420

348951

-

Pyruvate dehydrogenase complex from broccoli and cauliflower

1982

Randall, D.D.

Methods Enzymol.

89

408-414

348954

6216392

Pyruvate dehydrogenase complex from Neurospora

1982

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

Methods Enzymol.

89

386-391

348955

7144580

Pyruvate dehydrogenase complex from bovine kidney and heart

1982

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

Methods Enzymol.

89

376-386

348959

7030741

Pyruvate dehydrogenase complex from bakers yeast. 2. Molecular structure, dissociation, and implications for the origin of mitochondria

1981

Kresze, G.B.; Ronft, H.

Eur. J. Biochem.

119

581-587

348961

6455499

Molecular cloning of the pyruvate dehydrogenase complex genes of Escherichia coli

1980

Guest, J.R.; Stephens, P.E.

J. Gen. Microbiol.

121

277-292

348964

-

Purification and some properties of the pyruvate dehydrogenase complex of Bacillus subtilis

1980

Visser, J.; Kester, H.; Huigen, A.

FEMS Microbiol. Lett.

9

227-232

348965

7458900

Purificaton of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and resolution of its four component polypeptides

1980

Henderson, C.E.; Perham, R.N.

Biochem. J.

189

161-172

348967

383998

Molecular weight and symmetry of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

1979

Danson, M.J.; Hale, G.; Johnson, P.; Perham, R.N.

J. Mol. Biol.

129

603-617

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

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

349029

4588679

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.

248

5282-5290

349039

8867378

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

1996

Hein, S.; Steinbuechel, A.

FEMS Microbiol. Lett.

136

231-238

349054

3241566

Purification of branched-chain keto acid dehydrogenase and lipoamide dehydrogenase-valine from Pseudomonas

1988

Sokatch, J.R.

Methods Enzymol.

166

342-350

349067

3571202

Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex

1987

Ono, K.; Hakozaki, M.; Kimura, A.; Kochi, H.

J. Biochem.

101

19-27

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

2269305

Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi

1990

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

Eur. J. Biochem.

194

863-869

393963

2253629

Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

1990

Borges, A.; Hawkins, C.F.; Packman, L.C.; Perham, R.N.

Eur. J. Biochem.

194

95-102

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

393965

2226451

Subcellular localisation of dihydrolipoamide dehydrogenase and detection of lipoic acid in bloodstream forms of Trypanosoma brucei

1990

Jackman, S.A.; Hough, D.W.; Danson, M.J.; Stevenson, K.J.; Opperdoes, F.R.

Eur. J. Biochem.

193

91-95

393966

2687245

Purification of a new dihydrolipoamide dehydrogenase from Escherichia coli

1989

Richarme, G.

J. Bacteriol.

171

6580-6585

393968

3149394

Isolation and properties of the branched-chain 2-keto acid and pyruvate dehydrogenase multienzyme complex from Bacillus subtilis

1988

Perham, R.N.; Lowe, P.N.

Methods Enzymol.

166

330-342

393969

9757113

Crystallization and preliminary X-ray analysis of pig E3, lipoamide dehydrogenase

1998

Toyoda, T.; Kobayashi, R.; Sekiguchi, T.; Koike, K.; Koike, M.; Takenaka, A.

Acta Crystallogr. Sect. D

54

982-985

393970

9538259

Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast

1998

Toyoda, T.; Suzuki, K.; Sekiguchi, T.; Reed, L.J.; Takenaka, A.

J. Biochem.

123

668-674

393971

2643922

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

1989

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

Arch. Biochem. Biophys.

268

409-425

393973

8487301

Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties

1993

Mattevi, A.; Obmolova, G.; Kalk, K.H.; van Berkel, W.J.; Hol, W.G.

J. Mol. Biol.

230

1200-1215

393974

-

Dihydrolipoamide dehydrogenase from the Thermoacidophilic archaebacterium Thermoplasma acidophilum

1987

Smith, L.D.; Bungard, S.J.; Danson, M.J.; Hough, D.W.

Biochem. Soc. Trans.

15

1097

393975

2821168

Cloning and characterization of the gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae

1987

Roy, D.J.; Dawes, I.W.

J. Gen. Microbiol.

133

925-933

393976

3663096

Dihydrolipoamide dehydrogenase from Trypanosoma brucei. Characterization and cellular location

1987

Danson, M.J.; Conroy, K.; McQuattie, A.; Stevenson, K.J.

Biochem. J.

243

661-665

393978

-

Dihydrolipoamide dehydrogenase from halophilic archaebacteria: purification and properties of the enzyme from Halobacterium halobium

1986

Danson, M.J.; McQuattie, A.; Stevenson, K.J.

Biochemistry

25

3880-3884

393980

6373365

Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases

1984

Delaney, R.; Burns, G.; Sokatch, J.R.

FEBS Lett.

168

265-270

393981

6426463

Dihydrolipoamide dehydrogenase from halophilic archaebacteria

1984

Danson, M.J.; Eisenthal, R.; Hall, S.; Kessell, S.R.; Williams, D.L.

Biochem. J.

218

811-818

393982

6688711

Multifunctionality of lipoamide dehydrogenase promotion of electron transferase reaction

1983

Tsai, C.S.; Wand, A.J.; Templeton, D.M.; Weiss, P.M.

Arch. Biochem. Biophys.

225

554-561

393984

6404748

Lipoamide dehydrogenase from bakers yeast. Improved purification and some molecular, kinetic, and immunochemical properties

1983

Heinrich, P.; Ronft, H.; Schartau, W.; Kresze, G.B.

Hoppe-Seyler's Z. Physiol. Chem.

364

41-50

393986

6896050

Intracellular distribution and biosynthesis of lipoamide dehydrogenase in rat liver

1982

Matuda, S.; Saheki, T.

J. Biochem.

91

553-561

393987

-

Inhibition of pyruvate dehydrogenase multienzyme complex from Escherichia coli with a bifunctional arsenoxide: selective inactivation of lipoamide dehydrogenase

1981

Adamson, S.R.; Stevenson, K.J.

Biochemistry

20

3420-3424

393988

7011812

Dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12. Comparative characterization of the free and the complex-bound component

1981

Schmincke-Ott, E.; Bisswanger, H.

Eur. J. Biochem.

114

413-420

393989

7547908

Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S

1995

Hopkins, N.; Williams, C.H., Jr.

Biochemistry

34

11757-11765

393990

497161

Lipoamide dehydrogenase from Malbranchea pulchella: isolation and characterization

1979

McKay, D.J.; Stevenson, K.J.

Biochemistry

18

4702-4707

393991

507807

Purification of lipoamide dehydrogenase from Ascaris muscle mitochondria and its relationship to NADH:NAD+ transhydrogenase activity

1979

Komuniecki, R.; Saz, H.J.

Arch. Biochem. Biophys.

196

239-247

393992

8193135

Modulation of the Oxidation-Reduction Potential of the Flavin in Lipoamide Dehydrogenase from Escherichia coli by Alteration of a Nearby Charged Residue, K53R

1994

Maeda-Yorita, K.; Russell, G.C.; Guest, J.R.; Massey, V.; Williams, C.H., Jr.

Biochemistry

33

6213-6220

393993

-

Flavin-containing dehydrogenases

1976

Williams, C.H.

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

13

89-173

393994

8904806

Identification and purification of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts

1996

Conner, M.; Krell, T.; Lindsay, J.G.

Planta

200

195-202

393995

4611884

solation and characterization of pyruvate dehydrogenase complex from brewer's yeast

1973

Wais, U.; Gillmann, U.; Ulrich, J.

Hoppe-Seyler's Z. Physiol. Chem.

354

1378-1388

393996

4581500

Purification of lipoamide dehydrogenase by affinity chromatography on propyllipoamide-glass columns

1973

Scouten, W.H.; Torok, F.; Gitomer, W.

Biochim. Biophys. Acta

309

521-524

393998

4385248

Purification and properties of lipoamide dehydrogenase from yeast, Candida krusei

1963

Kawahara, Y.; Misaka, E.; Nakanishi, K.

J. Biochem.

63

77-82

393999

4323856

Microbial lipoamide dehydrogenase. Purification and some characteristics of the enzyme derived from selected microorganisms

1971

Scouten, W.H.; McManus, I.R.

Biochim. Biophys. Acta

227

248-263

394000

5769986

Brain lipoyl dehydrogenase. Purification, properties, and inhibitors

1969

Millard, S.A.; Kubose, A.; Gal, E.M.

J. Biol. Chem.

244

2511-2515

394001

-

Isolation und Eigenschaften von Liponsäuredehydrogenase aus Chloroplasten

1968

Jacobi, G.; Öhlers, U.

Z. Pflanzenphysiol.

58

193-206

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

394003

7797549

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

1995

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

J. Biol. Chem.

270

15545-15550

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

394005

11972781

Characterization of the dihydrolipoamide dehydrogenase from Streptococcus pneumoniae and its role in pneumococcal infection

2002

Smith, A.W.; Roche, H.; Trombe, M.C.; Briles, D.E.; Hakansson, A.

Mol. Microbiol.

44

431-448

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

394008

9217012

Isolation, partial characterization and localization of a dihydrolipoamide dehydrogenase from the cyanobacterium Synechocystis PCC 6803

1997

Engels, A.; Kahmann, U.; Ruppel, H.G.; Pistorius, E.K.

Biochim. Biophys. Acta

1340

33-44

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

394010

11495999

Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular and physiological analysis of the lpd gene and characterization of the enzyme

2001

Schwinde, J.W.; Hertz, P.F.; Sahm, H.; Eikmanns, B.J.; Guyonvarch, A.

Microbiology

147

2223-2231

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

2882-2889

394012

10806386

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structure of H- and L-proteins

2000

Faure, M.; Bourguignon, J.; Neuburger, M.; MacHerel, D.; Sieker, L.; Ober, R.; Kahn, R.; Cohen-Addad, C.; Douce, R.

Eur. J. Biochem.

267

2890-2898

394815

4387058

Rat-liver thiol: protein-disulphide oxidoreductase

1968

Spolter, P.D.; Vogel, J.M.

Biochim. Biophys. Acta

167

525-537

486166

2121129

Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli

1990

Ali, S.T.; Guest, J.R.

Biochem. J.

271

139-145

486167

2192914

Expression in Escherichia coli of a sub-gene encoding the lipoyl domain of the pyruvate dehydrogenase complex of Bacillus stearothermophilus [published erratum appears in FEBS Lett 1990 Jul 30;268(1):306]

1990

Dardel, F.; Packman, L.C.; Perham, R.N.

FEBS Lett.

264

206-210

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

486169

3050999

Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae

1988

Niu, X.D.; Browning, K.S.; Behal, R.H.; Reed, L.J.

Proc. Natl. Acad. Sci. USA

85

7546-7550

486170

2653824

The gene encoding dihydrolipoyl transacetylase from Azotobacter vinelandii. Expression in Escherichia coli and activation and isolation of the protein

1989

Hanemaaijer, R.; Westphal, A.H.; Berg, A.; van Dongen, W.; de Kok, A.; Veeger, C.

Eur. J. Biochem.

181

47-53

486171

3292237

The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis

1988

Hanemaaijer, R.; Janssen, A.; de Kok, A.; Veeger, C.

Eur. J. Biochem.

174

593-599

486172

2917567

The quaternary structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. A reconsideration

1989

Hanemaaijer, R.; Westphal, A.H.; van der Heiden, T.; de Kok, A.; Veeger, C.

Eur. J. Biochem.

179

287-292

486173

3691494

The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii

1987

Hanemaaijer, R.; de Kok, A.; Jolles, J.; Veeger, C.

Eur. J. Biochem.

169

245-252

486174

2917967

Separation of protein X from the dihydrolipoyl transacetylase component of the mammalian pyruvate dehydrogenase complex and function of protein X

1989

Powers-Greenwood, S.L.; Rahmatullah, M.; Radke, G.A.; Roche, T.E.

J. Biol. Chem.

264

3655-3657

486175

2914903

Subunit associations in the mammalian pyruvate dehydrogenase complex. Structure and role of protein X and the pyruvate dehydrogenase component binding domain of the dihydrolipoyl transacetylase component

1989

Rahmatullah, M.; Gopalakrishnan, S.; Andrews, P.C.; Chang, C.L.; Radke, G.A.; Roche, T.E.

J. Biol. Chem.

264

2221-2227

486176

2642901

Domain structures of the dihydrolipoyl transacetylase and the protein X components of mammalian pyruvate dehydrogenase complex. Selective cleavage by protease Arg C

1989

Rahmatullah, M.; Gopalakrishnan, S.; Radke, G.A.; Roche, T.E.

J. Biol. Chem.

264

1245-1251

486177

3169263

Time-resolved fluorescence studies on the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii

1988

Hanemaaijer, R.; Masurel, R.; Visser, A.J.W.G.; de Kok, A.; Veeger, C.

FEBS Lett.

238

285-288

486178

3421911

Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus

1988

Packman, L.C.; Borges, A.; Perham, R.N.

Biochem. J.

252

79-86

486179

3036145

Isolation of a cDNA clone for the dihydrolipoamide acetyltransferase component of the human liver pyruvate dehydrogenase complex

1987

Thekkumkara, T.J.; Jesse, B.W.; Ho, L.; Raefsky, C.; Pepin, R.A.; Javed, A.A.; Pons, G.; Patel, M.S.

Biochem. Biophys. Res. Commun.

145

903-907

486180

2950858

Molecular cloning of cDNA for rat liver lipoate acetyltransferase. A component of pyruvate dehydrogenase complex

1987

Matuda, S.; Matuo, S.; Nakano, K.; Saheki, T.

Biochem. Biophys. Res. Commun.

142

953-957

486181

3903169

Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli

1985

Guest, J.R.; Lewis, H.M.; Graham, L.D.; Packman, L.C.; Perham, R.N.

J. Mol. Biol.

185

743-754

486184

3919704

Limited proteolysis of the pyruvate dehydrogenase multienzyme complex of Bacillus subtilis

1985

Lowe, P.N.; Hodgson, J.A.; Perham, R.N.

Biochem. J.

225

249-253

486185

6714233

The size of the pyruvate dehydrogenase complex of Azotobacter vinelandii. Association phenomena

1984

Bosma, H.J.; de Kok, A.; van Markwijk, B.W.; Veeger, C.

Eur. J. Biochem.

140

273-280

486186

6430694

Repeating functional domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli

1984

Packman, L.C.; Hale, G.; Perham, R.N.

EMBO J.

3

1315-1319

486192

7030782

Pyruvate dehydrogenase multienzyme complex of Escherichia coli: determination of the Mr of the lipoate acetyltransferase component

1981

Danson, M.J.; Porteous, C.E.

FEBS Lett.

133

112-114

486194

6778866

Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from bovine heart

1981

Bleile, D.M.; Hackert, M.L.; Pettit, F.H.; Reed, L.J.

J. Biol. Chem.

256

514-519

486195

6780350

Bovine kidney pyruvate dehydrogenase complex. Limited proteolysis and molecular structure of the lipoate acetyltransferase component

1980

Kresze, G.B.; Ronft, H.

Eur. J. Biochem.

112

589-599

486196

6893315

Subunit structure of dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex from bovine kidney

1980

Machicao, F.; Wieland, O.H.

Hoppe-Seyler's Z. Physiol. Chem.

361

1093-1106

486197

6768590

Mammalian lipoate acetyltransferase: molecular weight determination by gel filtration in the presence of guanidinium chloride

1980

Kresze, G.B.; Dietl, B.; Ronft, H.

FEBS Lett.

112

48-50

486198

388441

Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli

1979

Bleile, D.M.; Munk, P.; Oliver, R.M.; Reed, L.J.

Proc. Natl. Acad. Sci. USA

76

4385-4389

486199

389239

Crystallization of a dihydrolipoyl transacetylase - dihydrolipoyl dehydrogenase subcomplex and its implications regarding the subunit structure of the pyruvate dehydrogenase complex from Escherichia coli

1979

Fuller, C.C.; Reed, L.J.; Oliver, R.M.; Hackert, M.L.

Biochem. Biophys. Res. Commun.

90

431-438

486201

1103138

Reconstitution of the Escherichia coli pyruvate dehydrogenase complex

1975

Reed, L.J.; Pettit, F.H.; Eley, M.H.; Hamilton, L.; Collins, J.H.; Oliver, R.M.

Proc. Natl. Acad. Sci. USA

72

3068-3072

486202

1194249

Purification properties and subunit composition of pig heart lipoate acetyltransferase

1975

Hamada, M.; Otsuka, K.I.; Tanaka, N.; Ogasahara, K.; Koike, K.; Hiraoka, T.; Koike, M.

J. Biochem.

78

187-197

486203

1089667

A kinetic study of dihydrolipoyl transacetylase from bovine kidney

1975

Butterworth, P.J.; Tsai, S.; Eley, M.H.; Roche, T.E.; Reed, L.J.

J. Biol. Chem.

250

1921-1925

486204

4584392

A new dihydrolipoamide transacetylase in Escherichia coli K12

1973

Bisswanger, H.; Henning, U.

Biochim. Biophys. Acta

321

143-148

486206

4934679

The subunit structure of the Escherichia coli K-12 pyruvate dehydrogenase complex. The dihydrolipoamide transacetylase component

1971

Vogel, O.; Beikirch, H.; Muller, H.; Henning, U.

Eur. J. Biochem.

20

169-178

486207

4900507

alpha-Keto acid dehydrogenase complexes. XII. Effects of acetylation on the activity and structure of the dihydrolipoyl transacetylase of Escherichia coli

1969

Schwartz, E.R.; Reed, L.J.

J. Biol. Chem.

244

6074-6079

486208

4866524

alpha-Keto acid dehydrogenase complexes. IX. Effects of iodination of the tyrosyl residues on the properties of the dihydrolipoyl transacetylase of Escherichia coli

1968

Schwartz, E.; Reed, L.J.

J. Biol. Chem.

243

639-643

486209

5335915

alpha-Keto acid dehydrogenase complexes. VII. Isolation and partial characterization of the polypeptide chains in the dihydrolipoyl transacetylase of Escherichia coli

1967

Henney, H.R.; Willms, C.R.; Muramatsu, T.; Mukherjee, B.B.; Reed, L.J.

J. Biol. Chem.

242

898-901

486210

5335914

alpha-Keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli

1967

Willms, C.R.; Oliver, R.M.; Henney, H.R.; Mukherjee, B.B.; Reed, L.J.

J. Biol. Chem.

242

889-897

486216

-

Isolation and characterization of a membrane-bound pyruvate dehydrogenase complex from the phototropic bacterium Rhodopseudomonas capsulata

1977

Luderitz, R.; Klemme, J.H.

Z. Naturforsch. C

32c

351-361

486217

7117532

Binding and dissociation of the pyruvate dehydrogenase complex of Azotobacter vinelandii on thiol--Sepharose

1982

De Graaf-Hess, A.C.; de Kok, A.

FEBS Lett.

143

261-264

486224

8958245

Cloning, sequencing, characterization and implications for vaccine design of the novel dihydrolipoyl acetyltransferase of Neisseria meningitidis

1996

Ala' Aldeen, D.A.A.; Westphal, A.H.; De Kok, A.; Weston, V.; Atta, M.S.; Baldwin, T.J.; Bartley, J.; Borriello, S.P.

J. Med. Microbiol.

45

419-432

486225

9280309

The catalytic domain of dihydrolipoyl acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Expression, purification and reversible denaturation

1997

Allen, M.D.; Perham, R.N.

FEBS Lett.

413

339-343

486226

11330694

Thermally induced changes of lipoate acetyltransferase inner core isolated from the Bacillus stearothermophilus pyruvate dehydrogenase complex

2001

Aso, Y.; Nakajima, A.; Meno, K.; Ishiguro, M.

Biosci. Biotechnol. Biochem.

65

698-701

486227

7890655

Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana

1995

Guan, Y.; Rawsthorne, S.; Scofield, G.; Shaw, P.; Doonan, J.

J. Biol. Chem.

270

5412-5417

486228

7703242

Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p)

1995

Hendle, J.; Mattevi, A.; Westphal, A.H.; Spee, J.; de Kok, A.; Teplyakov, A.; Hol, W.G.

Biochemistry

34

4287-4298

486229

-

Heterologously expressed inner lipoyl domain of dihydrolipoyl acetyltransferase inhibits ATP-dependent inactivation of pyruvate dehydrogenase complex, Identification of important amino acid residues

1998

Jackson, J.C.; Vinluan, C.C.; Dragland, C.J.; Sundararajan, V.; Yan, B.; Gounarides, J.S.; Nirmala, N.R.; Topiol, S.; Ramage, P.; Blume, J.E.; Aicher, T.D.; Bell, P.A.; Mann, W.R.

Biochem. J.

334

703-711

486230

8805537

Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase

1996

Mande, S.S.; Sarfaty, S.; Allen, M.D.; Perham, R.N.; Hol, W.G.J.

Structure

4

277-286

486231

9184165

Refolding and reconstitution studies on the transacetylase-protein X (E2/X) subcomplex of the mammalian pyruvate dehydrogenase complex: Evidence for specific binding of the dihydrolipoamide dehydrogenase component to sites on reassembled E2

1997

McCartney, R.G.; Sanderson, S.J.; Lindsay, J.G.

Biochemistry

36

6819-6826

486232

10491147

Characterization of the dihydrolipoamide acetyltransferase of the mitochondrial pyruvate dehydrogenase complex from potato and comparisons with similar enzymes in diverse plant species

1999

Millar, A.H.; Leaver, C.J.; Hill, S.A.

Eur. J. Biochem.

264

973-981

486233

10364395

Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) from Arabidopsis

1999

Mooney, B.P.; Miernyk, J.A.; Randall, D.D.

Plant Physiol.

120

443-452

486235

8504083

Sizing of bovine heart and kidney pyruvate dehydrogenase complex and dihydrolipoyl transacetylase core by quasielastic light scattering

1993

Roche, T.E.; Powers-Greenwood, S.L.; Shi, W.F.; Zhang, W.B.; Ren, S.Z.; Roche, E.D.; Cox, D.J.; Sorensen, C.M.

Biochemistry

32

5629-5637

486236

1935951

The catalytic domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli. Expression, purification, properties and preliminary X-ray analysis

1991

Schulze, E.; Westphal, A.H.; Obmolova, G.; Mattevi, A.; Hol, W.G.; de Kok, A.

Eur. J. Biochem.

201

561-568

486237

1554745

Purification and cellular localization of wild type and mutated dihydrolipoyltransacetylases from Azotobacter vinelandii and Escherichia coli expressed in E. coli

1992

Schulze, E.; Westphal, A.H.; Veenhuis, M.; de Kok, A.

Biochim. Biophys. Acta

1120

87-96

486238

10419491

The dihydrolipoamide S-acetyltransferase subunit of the mitochondrial pyruvate dehydrogenase complex from maize contains a single lipoyl domain

1999

Thelen, J.J.; Muszynski, M.G.; David, N.R.; Luethy, M.H.; Elthon, T.E.; Miernyk, J.A.; Randall, D.D.

J. Biol. Chem.

274

21769-21775

486239

12108679

Molecular cloning, and characterization and expression of dihydrolipoamide acetyltransferase component of murine pyruvate dehydrogenase complex in bile duct cancer cells

2002

Wang, L.; Kaneko, S.; Kagaya, M.; Ohno, H.; Honda, M.; Kobayashi, K.

J. Gastroenterol.

37

449-454

486240

9045657

Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex

1997

Yang, D.; Song, J.; Wagenknecht, T.; Roche, T.E.

J. Biol. Chem.

272

6361-6369

487333

4942179

Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex

1971

Derosier, D.J.; Oliver, R.M.; Reed, L.J.

Proc. Natl. Acad. Sci. USA

68

1135-1137

487335

4611273

A continuous spectrophotometric assay for the transacylase (E2) component of pyruvate and alpha-oxoglutarate dehydrogenase enzyme complexes

1974

Hall, E.R.; Weitzman, P.D.J.

Anal. Biochem.

62

286-290

487336

4588692

Mammalian alpha-keto acid dehydrogenase complexes. 8. Properties and subunit composition of the pig heart lipoate succinyltransferase

1974

Tanaka, N.; Koike, K.; Otsuka, K.I.; Hamada, M.; Ogasahara, K.; Koike, M.

J. Biol. Chem.

249

191-198

487337

391269

Structural and mechanistic studies of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli

1979

Angelides, K.J.; Hammes, G.G.

Biochemistry

18

5531-5537

487339

6770865

Lipoic acid content of dihydrolipoyl transacylases determined by isotope dilution analysis

1980

White, R.H.; Bleile, D.M.; Reed, L.J.

Biochem. Biophys. Res. Commun.

94

78-84

487340

1554728

Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli

1992

Robien, M.A.; Clore, G.M.; Omichinski, J.G.; Perham, R.N.; Appella, E.; Sakaguchi, K.; Gronenborn, A.M.

Biochemistry

31

3463-3471

487341

8076640

Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex

1994

Nakano, K.; Takase, C.; Sakamoto, T.; Nakagawa, S.; Inazawa, J.; Ohta, S.; Matuda, S.

Eur. J. Biochem.

224

179-189

487343

8899428

Different distribution of dihydrolipoamide succinyltransferase, dihydrolipoamide acetyltransferase and ATP synthase beta-subunit in monkey brain

1996

Takase, C.; Nakano, K.; Ohta, S.; Nakagawa, S.; Matuda, S.

In Vivo

10

495-502

487344

9405249

A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle

1997

Matuda, S.; Kodama, J.; Goshi, N.; Takase, C.; Nakano, K.; Nakagawa, S.; Ohta, S.

Biochem. Biophys. Res. Commun.

241

151-156

487345

9620315

Immunoreactivity of porcine heart dihydrolipoamide acetyl- and succinyl-transferases (PDC-E2, OGDC-E2) with primary biliary cirrhosis sera: characterization of the autoantigenic region and effects of enzymic delipoylation and relipoylation

1998

Koike, K.; Ishibashi, H.; Koike, M.

Hepatology

27

1467-1474

487346

10524791

Characterization of the Coxiella burnetii sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase

1999

Nguyen, S.V.; To, H.; Yamaguchi, T.; Fukushi, H.; Hirai, K.

Microbiol. Immunol.

43

743-749

487347

10739245

Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase

2000

Knapp, J.E.; Carroll, D.; Lawson, J.E.; Ernst, S.R.; Reed, L.J.; Hackert, M.L.

Protein Sci.

9

37-48

487348

10806400

Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex

2000

Koike, K.; Suematsu, T.; Ehara, M.

Eur. J. Biochem.

267

3005-3016

487349

11553602

Cloning, nucleotide sequence, and expression of the Brucella melitensis sucB gene coding for an immunogenic dihydrolipoamide succinyltransferase homologous protein

2001

Zygmunt, M.S.; Diaz, M.A.; Teixeira-Gomes, A.P.; Cloeckaert, A.

Infect. Immun.

69

6537-6540

644839

6746648

Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain alpha-keto acid dehydrogenase

1984

Chuang, D.T.; Hu, C.C.; Ku, L.S.; Niu, W.L.; Myers, D.E.; Cox, R.P.

J. Biol. Chem.

259

9277-9284

644842

1943690

Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex

1991

Chuang, D.T.; Fisher, C.W.; Lau, K.S.; Griffin, T.A.; Wynn, R.M.; Cox, R.P.

Mol. Biol. Med.

8

49-63

644846

10966480

Swinging arms and swinging domains in multifunctional emzymes: catalytic machines for multistep reactions

2000

Perham, R.N.

Annu. Rev. Biochem.

69

961-1004

644848

12031470

Characterization of rainbow trout branched-chain alpha-keto acid dehydrogenase complex: inter-domain segments of the E2 component affect the overall activity

2002

Hakozaki, M.; Ono, K.; Suzuki, T.; Hata, H.; Mori, T.; Kochi, H.

Comp. Biochem. Physiol. B Biochem. Mol. Biol.

132

433-442

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

657980

12590611

Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level

2003

Argyrou, A.; Sun, G.; Palfey, B.A.; Blanchard, J.S.

Biochemistry

42

2218-2228

659101

15826505

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

2005

Kim, H.

J. Biochem. Mol. Biol.

38

248-252

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

659482

15888450

Novelty of the pyruvate metabolic enzyme dihydrolipoamide dehydrogenase in spermatozoa: Correlation of its localization, tyrosine phosphorylation and activity during sperm capacitation

2005

Mitra, K.; Rangaraj, N.; Shivaji, S.

J. Biol. Chem.

280

25743-25753

667913

17083960

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

672465

-

Drosophila dihydrolipoamide dehydrogenase. Protein structure. Developmental expression

2005

Ivanova, P.; Harizanova, N.; Krasteva, M.; Dimov, S.V.; Ralchev, K.

Biokhimiya, Biofizika, Molekulyarnaya Biologiya i Genetika, Mikrobiologiya i Fiziologiya

96

115-123

672869

-

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

2006

Kim, H.

Bull. Korean Chem. Soc.

27

819-820

673190

17017892

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

2006

Gutierrez-Correa, J.

Curr. Drug Targets

7

1155-1179

673517

17110466

Dihydrolipoyl dehydrogenase as a source of reactive oxygen species inhibited by caloric restriction and involved in Saccharomyces cerevisiae aging

2007

Tahara, E.B.; Barros, M.H.; Oliveira, G.A.; Netto, L.E.; Kowaltowski, A.J.

FASEB J.

21

274-283

673943

15712224

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

2005

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

Hum. Mutat.

25

323-324

674368

16861247

Thermal unfolding process of dihydrolipoamide dehydrogenase studied by fluorescence spectroscopy

2006

Nishimoto, E.; Aso, Y.; Koga, T.; Yamashita, S.

J. Biochem.

140

349-357

674382

16584639

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

2006

Kim, H.

J. Biochem. Mol. Biol.

39

223-227

674430

15710613

pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification

2005

Klyachko, N.L.; Shchedrina, V.A.; Efimov, A.V.; Kazakov, S.V.; Gazaryan, I.G.; Kristal, B.S.; Brown, A.M.

J. Biol. Chem.

280

16106-16114

674479

16093239

Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis

2005

Rajashankar, K.R.; Bryk, R.; Kniewel, R.; Buglino, J.A.; Nathan, C.F.; Lima, C.D.

J. Biol. Chem.

280

33977-33983

674759

16263718

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

2006

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

J. Biol. Chem.

281

648-655

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

675350

15946682

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

2005

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

J. Mol. Biol.

350

543-552

677161

16442803

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

2006

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

Structure

14

611-621

691036

17706936

Valproic acid metabolites inhibit dihydrolipoyl dehydrogenase activity leading to impaired 2-oxoglutarate-driven oxidative phosphorylation

2007

Luis, P.B.; Ruiter, J.P.; Aires, C.C.; Soveral, G.; de Almeida, I.T.; Duran, M.; Wanders, R.J.; Silva, M.F.

Biochim. Biophys. Acta

1767

1126-1133

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

691569

-

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

2007

Kim, H.

Bull. Korean Chem. Soc.

28

907-908

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

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

693271

17960497

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

2008

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

J. Biomed. Sci.

15

37-46

693975

18316113

Changes in dihydrolipoamide dehydrogenase expression and activity during postnatal development and aging in the rat brain

2008

Yan, L.J.; Thangthaeng, N.; Forster, M.J.

Mech. Ageing Dev.

129

282-290

711099

20385101

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

2010

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

Biochem. Biophys. Res. Commun.

395

416-419

711225

20078138

Triazaspirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase

2010

Bryk, R.; Arango, N.; Venugopal, A.; Warren, J.D.; Park, Y.H.; Patel, M.S.; Lima, C.D.; Nathan, C.

Biochemistry

49

1616-1627

712087

20601046

Roles of dihydrolipoamide dehydrogenase Lpd1 in Candida albicans filamentation

2010

Kim, S.Y.; Kim, J.

Fungal Genet. Biol.

47

782-788

712097

20097961

Lipoamide dehydrogenase and diaphorase catalyzed conversion of some NO donors to NO and reduction of NO scavenger 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTIO)

2009

Stibingerova, A.; Velvarska, H.; Kynclova, K.; Marounkova, B.; Spundova, M.; Entlicher, G.

Gen. Physiol. Biophys.

28

384-390

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

724686

-

Characterization of two site-specific mutations in human dihydrolipoamide dehydrogenase

2013

Kim, H.

Bull. Korean Chem. Soc.

34

1621-1622

727213

10397837

Expression, reactivation, and purification of enzymes from Haloferax volcanii in Escherichia coli.

1999

Connaris, H.; Chaudhuri, J.B.; Danson, M.J.; Hough, D.W.

Biotechnol. Bioeng.

64

38-45

727409

9346289

Site-directed mutagenesis and halophilicity of dihydrolipoamide dehydrogenase from the halophilic archaeon, Haloferax volcanii

1997

Jolley, K.A.; Russell, R.J.; Hough, D.W.; Danson, M.J.

Eur. J. Biochem.

248

362-368

727729

8655478

Dihydrolipoamide dehydrogenase from the halophilic archaeon Haloferax volcanii: homologous overexpression of the cloned gene

1996

Jolley, K.A.; Rapaport, E.; Hough, D.W.; Danson, M.J.; Woods, W.G.; Dyall-Smith, M.L.

J. Bacteriol.

178

3044-3048

741757

24012808

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

2013

Ambrus, A.; Adam-Vizi, V.

Arch. Biochem. Biophys.

538

145-155

741807

27544700

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

2015

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

Biochem. Biophys. Rep.

2

50-56

741998

27544700

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

2016

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

Biochim. Biophys. Acta

1862

2098-2109

742087

25517164

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

2014

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

Biophys. J.

107

2993-3007

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

742221

-

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

2014

Kim, H.

Bull. Korean Chem. Soc.

35

1603-1604

742909

28174304

The pyruvate and alpha-ketoglutarate dehydrogenase complexes of Pseudomonas aeruginosa catalyze pyocyanin and phenazine-1-carboxylic acid reduction via the subunit dihydrolipoamide dehydrogenase

2017

Glasser, N.R.; Wang, B.X.; Hoy, J.A.; Newman, D.K.

J. Biol. Chem.

292

5593-5607

743008

25757537

Conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity

2015

Fukamichi, T.; Nishimoto, E.

J. Fluoresc.

25

577-583

743050

-

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

2015

Kim, H.

J. Korean Chem. Soc.

59

183-187

743051

-

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

2015

Kim, H.

J. Korean Chem. Soc.

59

344-348

743052

-

Characterization of human dihydrolipoamide dehydrogenase mutant with significantly decreased catalytic power

2016

Kim, H.

J. Korean Chem. Soc.

60

378-382

743127

28247484

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

2017

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

J. Mol. Recognit.

30

e2617

743450

23961884

The metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial lipoamide dehydrogenase2, a key enzyme in oxidative metabolism

2014

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

Plant Cell Environ.

37

684-695

755867

26428234

Mutagenesis of conserved active site residues of dihydrolipoamide succinyltransferase enhances the accumulation of alpha-ketoglutarate in Yarrowia lipolytica

2016

Guo, H.; Madzak, C.; Du, G.; Zhou, J.

Appl. Microbiol. Biotechnol.

100

649-659

758317

28391181

Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi

2017

Meireles, D.; Domingos, R.; Gaiarsa, J.; Ragnoni, E.; Bannitz-Fernandes, R.; da Silva Neto, J.; de Souza, R.; Netto, L.

Redox Biol.

12

600-609

763920

30717346

Chronic inhibition of mitochondrial dihydrolipoamide dehydrogenase (DLDH) as an approach to managing diabetic oxidative stress

2019

Yang, X.; Song, J.; Yan, L.J.

Antioxidants (Basel)

8

32

764703

29908278

Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase

2018

Szabo, E.; Mizsei, R.; Wilk, P.; Zambo, Z.; Torocsik, B.; Weiss, M.S.; Adam-Vizi, V.; Ambrus, A.

Free Radic. Biol. Med.

124

214-220

764862

29466712

Dihydrolipoamide dehydrogenase from Leishmania donovani New insights through biochemical characterization

2018

Chiranjivi, A.K.; Dubey, V.K.

Int. J. Biol. Macromol.

112

1241-1247

764880

32750477

Mutational studies on Leishmania donovani dihydrolipoamide dehydrogenase (LdBPK291950.1) indicates that the enzyme may not be classical class-I pyridine nucleotide-disulfide oxidoreductase

2020

Chiranjivi, A.K.; Prakash, J.; Saha, G.; Chandra, P.; Dubey, V.K.

Int. J. Biol. Macromol.

164

2141-2150

765207

-

Characterization of two site-specific mutations in human dihydrolipoamide dehydrogenase deteriorating the apparent enzyme binding affinities to both dihydrolipoamide and NAD+

2018

Kim, H.

J. Korean Chem. Soc.

62

253-256

765208

-

Characterization of human dihydrolipoamide dehydrogenase mutant showing significantly decreased catalytic efficiency

2019

Kim, H.

J. Korean Chem. Soc.

63

134-137

765209

-

Characterization of a human dihydrolipoamide dehydrogenase mutant showing significantly decreased catalytic efficiency toward NAD+

2020

Kim, H.

J. Korean Chem. Soc.

64

141-144

765210

-

Characterization of a site-specifically modified human dihydrolipoamide dehydrogenase mutant showing significantly changed kinetic properties

2021

Kim, H.

J. Korean Chem. Soc.

65

83-87

765736

32761961

Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent

2020

Dayan, A.; Yeheskel, A.; Lamed, R.; Fleminger, G.; Ashur-Fabian, O.

Proteins

89

21-28

Links to other databases for dihydrolipoamide

top print hide

Show Links (1 entry)

ChEBI

PubChem