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Ligand 3-mercaptopyruvate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 3-mercaptopyruvate

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Roles as Enzyme Ligand

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

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.8.1.2

3-mercaptopyruvate + cyanide = H2S + ?

690476

-

2.8.1.2

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate

723958, 724194, 645548, 645495, 645559, 713731, 725310, 645547, 645550, 645551, 645554, 645561, 645562, 645564, 645552, 645553, 645556, 645557, 645566, 645567, 645560, 645558, 645498, 645565, 645569, 738551, 739651, 739661, 645563, 738988, 739470, 645568, 725528, 738634

-

2.8.1.2

3-mercaptopyruvate + HSO3- = pyruvate + S2O32-

738198

-

2.8.1.2

3-mercaptopyruvate + thioredoxin = pyruvate + persulfurated thioredoxin

738988

-

2.8.1.2

4 entries

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

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.2

L-Cys + H2O + O2 = 2-oxo-3-mercaptopropanoic acid + NH3 + H2O2

0

-

1.4.3.3

D-cysteine + H2O + O2 = 2-oxo-3-thiopropionic acid + NH3 + H2O2

0

-

2.6.1.3

L-cysteine + 2-oxoglutarate = L-glutamate + beta-mercaptopyruvate

639955, 639954

-

Substrate in Enzyme-catalyzed Reactions (25 results)

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Show Substrate (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.24

L-ornithine + 3-mercaptopyruvic acid + NADPH + H+ = ? + NADP+ + H2O

712294

-

2.6.1.15

L-glutamine + 3-mercaptopyruvate = 2-oxoglutaramate + L-cysteine

639897, 639898

-

2.6.1.7

L-kynurenine + mercaptopyruvate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-cysteine

658649

-

2.6.1.7

L-kynurenine + mercaptopyruvate = ?

702779, 705702, 746952

-

2.6.1.7

L-kynurenine + mercaptopyruvate = kynurenic acid + ?

721881

-

2.8.1.1

3-mercaptopyruvate + 2 glutathione = pyruvate + glutathione disulfide

762111

-

2.8.1.1

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate

762459

-

2.8.1.1

cyanide + 3-mercaptopyruvate = ?

645520

-

2.8.1.2

3-mercaptopyruvate + 2 glutathione = pyruvate + glutathione disulfide

762111

-

2.8.1.2

3-mercaptopyruvate + 2-mercaptoethanol = ?

725528

-

2.8.1.2

3-mercaptopyruvate + 2-mercaptoethanol = pyruvate + ?

704585

-

2.8.1.2

3-mercaptopyruvate + cyanide = H2S + ?

690476

-

2.8.1.2

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate

723958, 724194, 645548, 645495, 645559, 713731, 725310, 645547, 645550, 645551, 645554, 645561, 645562, 645564, 645552, 645553, 645556, 645557, 645566, 645567, 645560, 645558, 645498, 645565, 645569, 738551, 739651, 739661, 645563, 738988, 739470, 645568, 725528, 738634, 762459

-

2.8.1.2

3-mercaptopyruvate + dihydrolipoic acid = ?

725528

-

2.8.1.2

3-mercaptopyruvate + dithiothreitol = ?

738896, 725528, 738634

-

2.8.1.2

3-mercaptopyruvate + glutathione = ?

725528

-

2.8.1.2

3-mercaptopyruvate + HSO3- = pyruvate + S2O3-

725310

-

2.8.1.2

3-mercaptopyruvate + HSO3- = pyruvate + S2O32-

738198

-

2.8.1.2

3-mercaptopyruvate + L-cysteine = ?

761523, 725528

-

2.8.1.2

3-mercaptopyruvate + L-homocysteine = ?

725528

-

2.8.1.2

3-mercaptopyruvate + N-acetyl-L-cysteine = ?

761523

-

2.8.1.2

3-mercaptopyruvate + thioredoxin = ?

725528

-

2.8.1.2

3-mercaptopyruvate + thioredoxin = pyruvate + persulfurated thioredoxin

760250, 761523, 738988

-

2.8.1.2

3-mercaptopyruvate + thiosulfate = pyruvate + H2S

724231

-

2.6.1.7

3 entries

2.8.1.1

3 entries

2.8.1.2

16 entries

2.8.1.4

3-mercaptopyruvate + activated tRNA = ? + S-tRNA

643805, 643808, 643812

-

Product in Enzyme-catalyzed Reactions (23 results)

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Show Product (23 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.5

L-cysteine + H2O + NAD+ = 3-mercapto-2-oxopropanoate + NH3 + NADH

0

-

1.4.1.8

L-cysteine + H2O + NAD+ = 3-mercapto-2-oxopropanoate + NH3 + NADH

0

-

1.4.3.2

L-Cys + H2O + O2 = 2-oxo-3-mercaptopropanoic acid + NH3 + H2O2

0

-

1.4.3.2

L-cysteine + H2O + O2 = 2-oxo-3-mercaptopropanoic acid + NH3 + H2O2

0

-

1.4.3.2

L-cystine + H2O + O2 = 2-oxo-3-mercaptopropanoic acid + NH3 + H2O2

0, 651026

-

1.4.3.2

L-cysteine + H2O + O2 = 2-oxo-3-thiopropanoate + NH3 + H2O2

0

-

1.4.3.2

4 entries

1.4.3.3

D-cysteine + H2O + O2 = 2-oxo-3-thiopropionic acid + NH3 + H2O2

0

-

1.4.99.6

D-cysteine + H2O + methylene blue = 3-mercapto-2-oxopropanoate + NH3 + reduced methylene blue

394974

-

1.4.99.B3

L-cysteine + H2O + 2 cytochrome b = 2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b

0

-

2.6.1.1

L-cysteine + 2-oxoglutarate = 3-mercaptopyruvate + L-glutamate

0

-

2.6.1.14

2-oxosuccinamic acid + L-cysteine = L-asparagine + 3-mercapto-2-oxopropanoate

0

-

2.6.1.15

2-oxoglutaramate + L-cysteine = L-glutamine + 3-mercapto-2-oxopropanoate

639898

-

2.6.1.15

glyoxylate + L-cysteine = glycine + 3-mercapto-2-oxopropanoate

639901, 639898

-

2.6.1.15

2 entries

2.6.1.3

L-cysteine + 2-oxoglutarate = L-glutamate + beta-mercaptopyruvate

639954, 639955

-

2.6.1.44

L-cysteine + pyruvate = 3-mercapto-2-oxopropanoate + L-alanine

0

-

2.6.1.5

L-cysteine + 2-oxoglutarate = 3-mercapto-2-oxopropanoate + L-glutamate

0, 640098

-

2.6.1.51

cysteine + pyruvate = 3-mercapto-2-oxo-propanoate + L-alanine

0

-

2.6.1.57

L-cysteine + alpha-ketomethiobutyrate = 2-oxo-3-thiopropanoate + L-methionine

636664

-

2.6.1.57

L-cysteine + 2-oxoglutarate = 3-mercaptopyruvate + L-glutamate

0

-

2.6.1.64

L-cysteine + glyoxylate = 3-mercapto-2-oxopropanoate + glycine

0

-

2.6.1.64

L-cysteine + phenylpyruvate = 3-mercapto-2-oxopropanoate + L-phenylalanine

0

-

2.6.1.57

2 entries

2.6.1.64

2 entries

2.6.1.7

L-cysteine + 2-oxobutanoate = 2-aminobutanoate + 3-mercapto-2-oxopropanoate

0

-

2.6.1.B23

L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate

0

-

Inhibitor in Enzyme-catalyzed Reactions (5 results)

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Show Inhibitors (5 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.197

-

347833, 347835

-

1.1.1.60

-

287164

-

2.6.1.15

-

639898

-

2.8.1.4

competitive inhibitor, supresses the transfer of sulfur to tRNA

643805

-

4.1.3.16

-

5253

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (36 results)

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Show Turnover Number (36 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.6.1.7

0.44

-

pH 7.5, 38°C

721881

2.6.1.7

3.28

-

in 100 mM boric acid buffer, pH 9.0, at 45°C

705702

2.6.1.7

3.59

-

in 100 mM potassium phosphate buffer (pH 7.4), at 37°C

702779

2.6.1.7

234

-

pH 7.5, 45°C

658649

2.8.1.1

0.7

-

pH 9

645520

2.8.1.1

1.2

-

pH 9

645520

2.8.1.1

54

-

pH 9

645520

2.8.1.2

0.05

-

mutant R178L, pH 8.0, 30°C

760250

2.8.1.2

0.068

-

mutant R178L/R187L, pH 8.0, 30°C

760250

2.8.1.2

0.0783

-

S249K mutant

645562

2.8.1.2

0.11

-

mutant S239A, pH 8.0, 30°C

760250

2.8.1.2

0.16

-

mutant R187L, pH 8.0, 30°C

760250

2.8.1.2

0.233

-

G248R mutant

645562

2.8.1.2

0.47

-

wild-type, pH 8.0, 30°C

760250

2.8.1.2

0.48

-

mutant H66A, pH 8.0, 30°C

760250

2.8.1.2

0.917

-

S249A mutant

645562

2.8.1.2

1

-

mutant D53A, pH 8.0, 30°C

760250

2.8.1.2

1.03

-

wild-type enzyme

645562

2.8.1.2

1.07

-

R196G mutant

645562

2.8.1.2

2.5

-

mutant S239A, pH 8.0, 30°C

760250

2.8.1.2

3.9

-

mutant H66A/R102L, pH 8.0, 30°C

760250

2.8.1.2

5.67

-

R187G mutant

645562

2.8.1.2

8.6

-

isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

8.8

-

isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

12.5

-

in the presence of cyanide, pH 9.55, 37°C

645548

2.8.1.2

20

-

mutant H66A, pH 8.0, 30°C

760250

2.8.1.2

20.2

-

isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

20.9

-

isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

25

-

pH 9.55

645564

2.8.1.2

30

-

MST2, 30°C

645565

2.8.1.2

49

-

mutant R102L, pH 8.0, 30°C

760250

2.8.1.2

59

-

mutant R102K, pH 8.0, 30°C

760250

2.8.1.2

75

-

mutant H66N, pH 8.0, 30°C

760250

2.8.1.2

112

-

wild-type, pH 8.0, 30°C

760250

2.8.1.2

165

-

MST1, 30°C

645565

2.8.1.2

2260

-

pH 8.4, 30°C

704585

2.6.1.7

4 entries

2.8.1.1

3 entries

2.8.1.2

29 entries

K_M Value (60 results)

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Show KM Value (60 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.6.1.15

4.8

-

pH 8.4, 37ºC

639898

2.6.1.64

0.61

-

pH 7.0, 30°C, L-glutamine as amino group donor

640172

2.6.1.7

2.4

-

in 100 mM boric acid buffer, pH 9.0, at 45°C

705702

2.6.1.7

2.5

-

pH 7.5, 45°C

658649

2.6.1.7

2.8

-

in 100 mM potassium phosphate buffer (pH 7.4), at 37°C

702779

2.6.1.7

3.2

-

pH 7.5, 38°C

721881

2.8.1.1

3.7

-

pH 9

645520

2.8.1.1

35.4

-

pH 9

645520

2.8.1.1

51.7

-

pH 9

645520

2.8.1.2

0.015

-

cosubstrate N-acetyl-L-cysteine, mitochondrial splice variant MPST2, Hill coefficient 1.1, pH 7.4, 37°C

761523

2.8.1.2

0.02

-

cosubstrate N-acetyl-L-cysteine, cytosolic splice variant MPST1, Hill coefficient 1.3, pH 7.4, 37°C

761523

2.8.1.2

0.02

-

glutathione as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.022

-

cosubstrate L-cysteine, mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 37°C

761523

2.8.1.2

0.022

-

using L-cysteine as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.024

-

cosubstrate L-cysteine, cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 37°C

761523

2.8.1.2

0.025

-

using dihydrolipioic acid as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.026

-

using dithiothreitol as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.03

-

using L-homocysteine as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.053

-

pH 8.4, 30°C

704585

2.8.1.2

0.13

-

using 2-mercaptoethanol as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.2

-

pH 7.3, 37°C

645569

2.8.1.2

0.24

-

mutant S239A, pH 8.0, 30°C

760250

2.8.1.2

0.35

-

using cyanide as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.35

-

using thioredoxin as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C

725528

2.8.1.2

0.358

-

cosubstrate thioredoxin, cytosolic splice variant MPST1, Hill coefficient 2.0, pH 7.4, 37°C

761523

2.8.1.2

0.36

-

cosubstrate thioredoxin, mitochondrial splice variant MPST2, Hill coefficient 2.1, pH 7.4, 37°C

761523

2.8.1.2

0.43

-

mutant H66A, pH 8.0, 30°C

760250

2.8.1.2

0.49

-

S249A mutant

645563

2.8.1.2

0.54

-

isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

0.55

-

isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

0.6

-

mutant S239A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C

760250

2.8.1.2

0.79

-

mutant H66A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C

760250

2.8.1.2

0.9

-

mutant R102L, pH 8.0, 30°C

760250

2.8.1.2

1

-

mutant H66A/R102L, pH 8.0, 30°C

760250

2.8.1.2

1

-

mutant R102K, pH 8.0, 30°C

760250

2.8.1.2

1

-

wild-type, pH 8.0, 30°C

760250

2.8.1.2

1.1

-

S249K mutant

645563

2.8.1.2

1.2

-

wild-type enzyme

645563

2.8.1.2

1.29

-

isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

1.33

-

isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C

738634

2.8.1.2

1.4

-

mutant H66N, pH 8.0, 30°C

760250

2.8.1.2

1.7

-

wild-type, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C

760250

2.8.1.2

2

3

mutant R178L/R187L, pH 8.0, 30°C

760250

2.8.1.2

2.1

-

G248R mutant

645563

2.8.1.2

2.4

-

mutant D53A, pH 8.0, 30°C

760250

2.8.1.2

4

-

mutant R187L, pH 8.0, 30°C

760250

2.8.1.2

4.08

-

pH 8, 30°C

645567

2.8.1.2

7.02

-

pH 8.0, 37°C

762459

2.8.1.2

7.3

-

cytosolic enzyme

645498

2.8.1.2

7.4

7.7

-

645551

2.8.1.2

7.6

-

mitochondrial enzyme

645498

2.8.1.2

8.34

-

determination of pyruvate formation, 37°C, pH 9.55

645548

2.8.1.2

11

-

MST1, 30°C

645565

2.8.1.2

11

-

R196G mutant

645563

2.8.1.2

12.5

-

determination of thiocyanate formation, 37°C, pH 9.55

645548

2.8.1.2

15

-

mutant R178L, pH 8.0, 30°C

760250

2.8.1.2

70

-

R187G mutant

645563

2.8.1.2

72

-

MST2, 30°C

645565

2.8.1.2

73

-

pH 9.6

645564

2.6.1.7

4 entries

2.8.1.1

3 entries

2.8.1.2

50 entries

2.8.1.4

0.0069

-

pH 7.8, 37°C

643805

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.8.1.4

0.005

-

pH 7.8, 37°C

643805

References & Links

Literature References (67)

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Show Reference (67 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5253

3966804

Rat liver 4-hydroxy-2-ketoglutarate aldolase: purification and kinetic characterization

1985

Anderson, M.; Scholtz, J.M.; Schuster, S.M.

Arch. Biochem. Biophys.

236

82-97

287164

4300866

Tartaric acid metabolism. 8. Crystalline tartronic semialdehyde reductase

1968

Kohn, L.

J. Biol. Chem.

243

4426-4433

347833

3575753

Glutathione mixed disulfide inhibitors of the human placental NADP-linked 15-hydroxyprostaglandin dehydrogenase

1987

Chung, H.; Fried, J.; Williams-Ashman, E.; Jarabak, J.

Prostaglandins

33

383-390

347835

1641503

NADP-dependent 15-hydroxyprostaglandin dehydrogenase is homologous to NAD-dependent 15-hydroxyprostaglandin dehydrogenase and other short-chain alcohol dehydrogenases

1992

Wermuth, B.

Prostaglandins

44

5-9

394974

-

D-Amino acid dehydrogenase (Pseudomonas fluorescens)

1971

Tsukada, K.

Methods Enzymol.

17B

623-624

636664

8633027

Aromatic amino acid transamination and methionine recycling in trypanosomatids

1996

Berger, B.J.; Dai, W.W.; Wang, H.; Stark, R.E.; Cerami, A.

Proc. Natl. Acad. Sci. USA

93

4126-4130

639897

3003500

Glutamine transaminase L from rat liver

1985

Cooper, A.J.L.; Meister, A.

Methods Enzymol.

113

338-343

639898

5059882

Isolation and properties of highly purified glutamine transaminase

1972

Cooper, A.J.L.; Meister, A.

Biochemistry

11

661-671

639901

4822504

Isolation and properties of a new glutamine transaminase form rat kidney

1974

Cooper, A.J.L.; Meister, A.

J. Biol. Chem.

249

2554-2561

639954

20209

Purification and partial characterization of cysteine-glutamate transaminase from rat liver

1977

Thibert, R.J.; Schmidt, D.E.

Can. J. Biochem.

55

958-964

639955

7113743

Purification and characterization of cysteine aminotransferase from rat liver cytosol

1982

Akagi, R.

Acta Med. Okayama

36

187-197

640098

4396841

Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase

1971

Miller, J.E.; Litwack, G.

J. Biol. Chem.

246

3234-3240

640172

1278181

Glutamine transaminase from brain tissue. Further studies on kinetic properties and specificity of the enzyme

1976

Van Leuven, F.

Eur. J. Biochem.

65

271-274

643805

4987417

Ribonucleic acid sulfurtransferase from Bacillus subtilis W168. Sulfuration with beta-mercaptopyruvate and properties of the enzyme system

1970

Wong, T.W.; Weiss, S.B.; Eliceiri, G.L.; Bryant, J.

Biochemistry

9

2376-2386

643808

4601536

Transfer ribonucleic acid sulfurtransferase isolated from rat cerebral hemispheres

1974

Wong, T.W.; Harris, M.A.; Jankowicz, C.A.

Biochemistry

13

2805-2812

643812

24834

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Links to other databases for 3-mercaptopyruvate

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