print visible entries

print all entries

Ligand oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (21 results)

top print hide

Show Substrate (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.5.10

D-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

763205

-

1.1.5.10

L-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

763205

-

1.1.5.12

(R)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + ?

763205

-

1.1.5.12

(R)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

761384

-

1.1.5.12

(S)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + ?

763205

-

1.1.5.12

(S)-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

761384

-

1.1.5.12

D-2-hydroxybutanoate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = 2-oxobutanoate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

761384

-

1.1.5.12

D-2-hydroxybutyrate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = 2-oxobutanoate + ?

763205

-

1.1.5.12

D-2-hydroxybutyrate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = ? + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

763205

-

1.1.5.12

D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = ?

763205

-

1.1.5.12

D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = ? + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

763205

-

1.1.5.12

D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = D-glyceraldehyde + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

761384

-

1.1.5.12

D-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

763205

-

1.1.5.12

L-lactate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = pyruvate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

763205

-

1.1.5.10

2 entries

1.1.5.12

12 entries

1.1.5.14

D-fructose + [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] = 5-dehydro-D-fructose + [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan

706060

-

1.10.5.1

N-methyldihydronicotinamide + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = N-methylnicotinamide + ?

724559

-

1.18.1.2

3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NADPH + H+ = ? + NADP+

727207

-

1.3.8.1

butyryl-CoA + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = 2-butenoyl-CoA + reduced acceptor

391308

-

1.5.99.13

D-proline + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = DELTA1-pyrroline 2-carboxylate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

394966

-

1.6.2.4

NADPH + H+ + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = NADP+ + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

711305, 743521

-

1.6.5.2

3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NAD(P)H = reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NAD(P)+

692722, 394383

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (20 results)

top print hide

Show Turnover Number (20 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.5.10

128

-

pH 7.4, 30°C

763205

1.1.5.12

5.3

-

cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C

761384

1.1.5.12

128

-

cosubstrate (R)-lactate, pH 7.4, 30°C

761384

1.1.5.12

128

-

pH 7.4, 30°C

763205

1.6.2.4

5.83

-

wild type enzyme, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

8.5

-

wild type enzyme, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

10.5

-

mutant enzyme D113A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

11.67

-

wild type enzyme, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

13

-

mutant enzyme E115A/E116A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

13.83

-

mutant enzyme D113A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

15.7

-

isoform CPR1, at pH 7.6 and 25°C

743521

1.6.2.4

18.3

-

mutant enzyme E115A/E116A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

18.3

-

wild type enzyme, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

20

-

mutant enzyme D113A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

25

-

mutant enzyme E115A/E116A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

28.3

-

wild type enzyme, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

30

-

mutant enzyme D113A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

38.3

-

mutant enzyme E115A/E116A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

40

-

mutant enzyme D113A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

56.67

-

mutant enzyme E115A/E116A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.1.5.12

3 entries

1.6.2.4

16 entries

K_M Value (19 results)

top print hide

Show KM Value (19 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.5.10

0.048

-

pH 7.4, 30°C

763205

1.1.5.12

0.031

-

cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C

761384

1.1.5.12

0.048

-

cosubstrate (R)-lactate, pH 7.4, 30°C

761384

1.1.5.12

0.048

-

pH 7.4, 30°C

763205

1.6.2.4

0.0018

-

mutant enzyme E115A/E116A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0021

-

mutant enzyme D113A, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0022

-

wild type enzyme, using 10 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0026

-

mutant enzyme D113A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0026

-

mutant enzyme E115A/E116A, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0031

-

wild type enzyme, using 30 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0038

-

mutant enzyme E115A/E116A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0039

-

wild type enzyme, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0041

-

mutant enzyme D113A, using 60 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0062

-

wild type enzyme, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0063

-

mutant enzyme D113A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0065

-

mutant enzyme E115A/E116A, using 110 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.0087

-

mutant enzyme D113A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.01

-

wild type enzyme, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.6.2.4

0.011

-

mutant enzyme E115A/E116A, using 210 mM oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide as substrate, in 20 mM HEPES buffer (pH 7.5), at 25°C

711305

1.1.5.12

3 entries

1.6.2.4

15 entries

References & Links

Literature References (11)

top print hide

Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

391308

9009069

NAD-independent lactate and butyryl-CoA dehydrogenases of Clostridium acetobutylicum P262

1997

Diez-Gonzalez, F.; Russell, J.B.; Hunter, J.B.

Curr. Microbiol.

34

162-166

394383

11238963

NAD(P)H:menadione oxidoreductase of the amitochondriate eukaryote Giardia lamblia: a simpler homologue of the vertebrate enzyme

2001

Sanchez, L.B.; Elmendorf, H.; Nash, T.E.; Muller, M.

Microbiology

147

561-570

394966

11823469

Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase

2002

Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T.

J. Biol. Chem.

277

12861-12867

692722

18512942

In vitro activity of almond skin polyphenols for scavenging free radicals and inducing quinone reductase

2008

Chen, C.Y.; Blumberg, J.B.

J. Agric. Food Chem.

56

4427-4434

706060

19506535

Direct spectrophotometric determination of serum fructose in pancreatic cancer patients

2009

Hui, H.; Huang, D.; McArthur, D.; Nissen, N.; Boros, L.G.; Heaney, A.P.

Pancreas

38

706-712

711305

20152939

Beta sheet 2-alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners

2010

Jang, H.H.; Jamakhandi, A.P.; Sullivan, S.Z.; Yun, C.H.; Hollenberg, P.F.; Miller, G.P.

Biochim. Biophys. Acta

1804

1285-1293

724559

23953689

Design, synthesis, biological and structural evaluation of functionalized resveratrol analogues as inhibitors of quinone reductase 2

2013

John, S.E.St.; Jensen, K.C.; Kang, S.; Chen, Y.; Calamini, B.; Mesecar, A.D.; Lipton, M.A.

Bioorg. Med. Chem.

21

6022-6037

727207

23586955

Biochemical characterization of two recombinant ferredoxin reductases from Alcanivorax borkumensis SK2

2012

Teimoori, A.; Ahmadian, S.; Madadkar-Sobhani, A.

Biotechnol. Appl. Biochem.

59

457-464

743521

24935229

Heterologous expression and functional characterization of the NADPH-cytochrome P450 reductase from Capsicum annuum

2014

Lee, G.Y.; Kim, H.M.; Ma, S.H.; Park, S.H.; Joung, Y.H.; Yun, C.H.

Plant Physiol. Biochem.

82

116-122

761384

28847921

A bacterial multidomain NAD-independent D-lactate dehydrogenase utilizes flavin adenine dinucleotide and Fe-S clusters as cofactors and quinone as an electron acceptor for D-lactate oxidization

2017

Jiang, T.; Guo, X.; Yan, J.; Zhang, Y.; Wang, Y.; Zhang, M.; Sheng, B.; Ma, C.; Xu, P.; Gao, C.

J. Bacteriol.

199

e00342

763205

28847921

A bacterial multidomain NAD-independent D-lactate dehydrogenase utilizes flavin adenine dinucleotide and Fe-S clusters as cofactors and quinone as an electron acceptor for D-lactate oxidization

2017

Jiang, T.; Guo, X.; Yan, J.; Zhang, Y.; Wang, Y.; Zhang, M.; Sheng, B.; Ma, C.; Xu, P.; Gao, C.

J. Bacteriol.

199

e00342-17

Links to other databases for oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

top print hide

Show Links (1 entry)

ChEBI

PubChem

-