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Ligand acetyl phosphate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

acetate fermentation, glycine metabolism, ornithine metabolism, purine metabolism, sulfate reduction

KEGG

Carbon fixation pathways in prokaryotes, Carbon metabolism, Methane metabolism, Microbial metabolism in diverse environments, Pyruvate metabolism, Taurine and hypotaurine metabolism more

MetaCyc

(S)-lactate fermentation to propanoate, acetate and hydrogen, acetate and ATP formation from acetyl-CoA I, acetylene degradation (anaerobic), Bifidobacterium shunt, ethanolamine utilization, gallate degradation III (anaerobic), glycine degradation (reductive Stickland reaction), heterolactic fermentation, L-lysine fermentation to acetate and butanoate, methanogenesis from acetate, mixed acid fermentation, purine nucleobases degradation I (anaerobic), purine nucleobases degradation II (anaerobic), pyruvate fermentation to acetate II, pyruvate fermentation to acetate IV, reductive glycine pathway, sulfoacetaldehyde degradation I, sulfolactate degradation II, superpathway of fermentation (Chlamydomonas reinhardtii) more

Show all BRENDA pathways known for acetyl phosphate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Natural Substrate (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.4.2

acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin

636464, 636465, 636466, 636467, 636469, 636470, 636476, 636477, 636471, 636472, 636473, 636475, 636474, 636462, 636468, 484935

-

2.3.1.32

acetyl phosphate + L-lysine = phosphate + N6-acetyl-L-lysine

486790

-

2.3.1.32

acetyl phosphate + L-ornithine = phosphate + N5-acetyl-L-ornithine

486790

-

2.3.1.32

2 entries

2.3.1.8

CoA + acetyl phosphate = acetyl-CoA + phosphate

695918, 675833

1xco, 3D-view

2.7.1.61

D-glucose + acetyl phosphate = D-glucose 6-phosphate + acetate

636972, 636973, 636974

-

2.7.2.1

ADP + acetyl phosphate = ATP + acetate

761931, 761116, 744070, 762441, 761006, 757471

-

2.7.2.12

acetyl phosphate + phosphate = acetate + diphosphate

762441

-

2.7.2.12

phosphate + acetyl phosphate = diphosphate + acetate

737773

-

2.7.2.12

2 entries

3.6.1.7

acetylphosphate + H2O = acetate + phosphate

758508

-

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

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Show Natural Product (16 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.3.3

2 pyruvate + phosphate + 2 O2 + H2O = acetate + acetyl phosphate + 2 CO2 + 2 H2O2

-

-

1.2.3.3

pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2

114312, 390433, 390437, 390435, , 390431, 390432, 390436, 390429, 390430

-

1.2.3.3

pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2

-

-

1.2.3.3

3 entries

1.21.4.2

glycine + phosphate + thioredoxin = acetyl phosphate + NH3 + thioredoxin disulfide + H2O

-

-

1.21.4.3

N-methylglycine + phosphate + thioredoxin = acetyl phosphate + methylamine + thioredoxin disulfide

-

-

1.21.4.4

N,N,N-trimethylglycine + phosphate + thioredoxin = acetyl phosphate + trimethylamine + thioredoxin disulfide

-

-

2.3.1.8

acetyl-CoA + phosphate = CoA + acetyl phosphate

, 487527, 487543, 487531, 487532, 94495, 487525, 487524, 487523, 487522, 487536, 487533, 487513, 487516, 487530, 487514, 487515, 487518, 487519, 487520, 487521, 487534, 487535, 487538, 487526, 487539, 487542, 487537, 487540, 487529, 487517

1xco, 3D-view

2.3.3.15

2-sulfoacetaldehyde + phosphate = acetyl phosphate + sulfite

-

-

2.7.2.1

ATP + acetate = ADP + acetyl phosphate

642182, , 642167, 642177, 642172, 642198, 642183, 642185, 642166, 642170, 642171, 642173, 642174, 642175, 642178, 642176, 642181, 642189, 642186, 642197, 642191, 642194, 642196, 487537, 642190, 642179, 642180, 642195, 642184

-

2.7.2.12

acetate + diphosphate = acetyl phosphate + phosphate

-

-

2.7.2.12

diphosphate + acetate = phosphate + acetyl phosphate

-

-

4.1.2.22

D-Fructose 6-phosphate + phosphate = Acetyl phosphate + D-erythrose 4-phosphate + H2O

-

-

4.1.2.22

D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate

-

-

4.1.2.22

D-Xylulose 5-phosphate + phosphate = Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O

-

-

4.1.2.9

D-Xylulose 5-phosphate + phosphate = Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O

-

-

4.1.2.9

D-xylulose 5-phosphate = pyruvate + acetyl phosphate

-

-

2.7.2.12

2 entries

4.1.2.22

3 entries

4.1.2.9

2 entries

Substrate in Enzyme-catalyzed Reactions (25 results)

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Show Substrate (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.4.2

acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin

636464, 636465, 636466, 636467, 636469, 636470, 636476, 636477, 636471, 636472, 636473, 636475, 636474, 636462, 636468, 484935

-

2.3.1.222

CoA + acetyl phosphate = acetyl-CoA + phosphate

756682, 719708

-

2.3.1.32

acetyl phosphate + L-lysine = phosphate + N6-acetyl-L-lysine

486790

-

2.3.1.32

acetyl phosphate + L-ornithine = phosphate + N5-acetyl-L-ornithine

486790

-

2.3.1.8

3'-dephospho-CoA + acetyl phosphate = acetyl-3'-dephospho-CoA + phosphate

487533

1xco, 3D-view

2.3.1.8

acetyl phosphate + CoA = acetyl-CoA + phosphate

720217, 719451, 720421, 720425

1xco, 3D-view

2.3.1.8

CoA + acetyl phosphate = acetyl-CoA + phosphate

674792, 756682, 695918, 675833

1xco, 3D-view

2.3.1.8

acetyl-phosphate + CoA = acetyl-CoA + phosphate

674262, 674263

1xco, 3D-view

2.3.1.32

2 entries

2.3.1.8

4 entries

2.7.1.146

acetyl-phosphate + D-fructose 6-phosphate = acetate + D-fructose 1,6-bisphosphate

395269

-

2.7.1.157

acetyl-phosphate + N-acetyl-alpha-D-galactosamine = acetate + N-acetyl-alpha-D-galactosamine 1-phosphate

659129

-

2.7.1.61

D-fructose + acetyl phosphate = D-fructose 1-phosphate + D-fructose 6-phosphate + acetate

636973, 636972

-

2.7.1.61

D-glucose + acetyl phosphate = D-glucose 6-phosphate + acetate

636972, 636973, 636974

-

2.7.1.61

D-mannitol + acetyl phosphate = ?

636972, 636973

-

2.7.1.61

D-mannose + acetyl phosphate = D-mannose 6-phosphate + acetate

636972, 636973

-

2.7.1.61

N-acetylglucosamine + acetyl phosphate = ?

636974

-

2.7.1.61

5 entries

2.7.1.77

acetylphosphate + inosine = acetate + IMP

642002

-

2.7.2.1

acetyl phosphate + hydroxylamine = acetyl hydroxamate + phosphate

659065, 659856, 659446, 738717, 739591, 691204

-

2.7.2.1

ADP + acetyl phosphate = ATP + acetate

761931, 761116, 744070, 762441, 761006, 757471, 746769

-

2.7.2.12

acetyl phosphate + phosphate = acetate + diphosphate

762441

-

2.7.2.12

phosphate + acetyl phosphate = diphosphate + acetate

722150, 744414, 737773, 642212

-

2.7.2.1

2 entries

2.7.2.12

2 entries

3.1.3.2

acetylphosphate + H2O = acetate + phosphate

134766, 134772

-

3.6.1.7

acetyl phosphate + H2O = acetate + phosphate

246781, 246800, 246778, 246775, 246795, 246799, 246787, 246792, 246785, 246784, 246786, 654097, 654100, 667658, 734482

-

3.6.1.7

acetylphosphate + H2O = acetate + phosphate

758508

-

3.6.1.7

2 entries

6.3.1.21

ADP + acetyl phosphate = ?

760556

-

7.6.2.1

acetyl phosphate + H2O = acetate + phosphate

246837

-

Product in Enzyme-catalyzed Reactions (44 results)

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Show Product (44 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.72

1-hydroxyethylphosphonate + O2 = acetylphosphate

-

-

1.2.1.12

acetaldehyde + phosphate + NAD+ = acetyl phosphate + NADH

-

-

1.2.3.3

2 pyruvate + phosphate + 2 O2 + H2O = acetate + acetyl phosphate + 2 CO2 + 2 H2O2

-

-

1.2.3.3

pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O = acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2

390430, 390437, 390429

-

1.2.3.3

pyruvate + phosphate + ferricyanide + H2O = acetyl phosphate + ferrocyanide + H2O2

, 390437

-

1.2.3.3

pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2

114312, 390433, 390437, , 390435, 390431, 390432, 390430, 390436, 390429

-

1.2.3.3

pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2

, 390429

-

1.2.3.3

5 entries

1.21.4.2

glycine + phosphate + thioredoxin = acetyl phosphate + NH3 + thioredoxin disulfide + H2O

-

-

1.21.4.3

N-methylglycine + phosphate + dithioerythritol = acetyl phosphate + methylamine + dithioerythritol disulfide

636280

-

1.21.4.3

N-methylglycine + phosphate + thioredoxin = acetyl phosphate + methylamine + thioredoxin disulfide

, 636282, 636280, 636281

-

1.21.4.3

2 entries

1.21.4.4

N,N,N-trimethylglycine + phosphate + thioredoxin = acetyl phosphate + trimethylamine + thioredoxin disulfide

, 636281

-

2.1.2.2

acetate + ATP = acetyl phosphate + ADP

-

-

2.3.1.19

acetyl-CoA + phosphate = acetyl Phosphate + CoA

-

-

2.3.1.19

acetyl-CoA + phosphate = CoA + acetyl phosphate

-

-

2.3.1.19

acetyl-CoA + phosphate = acetylphosphate + CoA

-

-

2.3.1.19

3 entries

2.3.1.222

acetyl-CoA + phosphate = CoA + acetyl phosphate

-

-

2.3.1.54

pyruvate + phosphate = acetylphosphate + formate

487218

-

2.3.1.8

acetyl-CoA + phosphate = acetyl Phosphate + CoA

-

1xco, 3D-view

2.3.1.8

acetyl-CoA + phosphate = CoA + acetyl phosphate

, 487527, 487543, 487531, 487532, 94495, 487525, 487524, 487523, 487522, 487536, 487533, 487513, 487516, 487530, 487514, 487515, 487518, 487519, 487520, 487521, 487534, 487535, 487538, 487526, 487539, 487542, 487537, 487540, 487529, 487517

1xco, 3D-view

2.3.1.8

2 entries

2.3.3.15

2-sulfoacetaldehyde + phosphate = acetyl phosphate + sulfite

-

-

2.7.2.1

ATP + acetate = ADP + acetyl phosphate

642182, , 642166, 642167, 642177, 642172, 642180, 642198, 642183, 642185, 642170, 642171, 642173, 642174, 642175, 642178, 642176, 642181, 642189, 642186, 642197, 642184, 642191, 642194, 642196, 487537, 642190, 642195, 642179

-

2.7.2.1

CTP + acetate = CDP + acetyl phosphate

642172, , 642176, 642189, 642184, 487537, 642179

-

2.7.2.1

GTP + acetate = GDP + acetyl phosphate

, 642182, 642172, 642180, 642173, 642178, 642176, 642181, 642189, 642184, 487537, 642179

-

2.7.2.1

ITP + acetate = IDP + acetyl phosphate

642182, 642166, , 642173, 642178, 642176, 642189, 642184, 487537, 642179

-

2.7.2.1

TTP + acetate = TDP + acetyl phosphate

642178, 642184,

-

2.7.2.1

UTP + acetate = UDP + acetyl phosphate

642172, , 642181, 642189, 487537, 642179

-

2.7.2.12

acetate + diphosphate = acetyl phosphate + phosphate

-

-

2.7.2.12

diphosphate + acetate = phosphate + acetyl phosphate

-

-

2.7.2.15

acetate + ATP = acetyl phosphate + ADP

-

-

2.7.2.15

ATP + acetate = ADP + acetyl phosphate

-

-

2.7.2.1

6 entries

2.7.2.12

2 entries

2.7.2.15

2 entries

2.7.2.18

ATP + acetate = ADP + acetyl phosphate

-

-

2.7.2.6

ATP + acetate = ADP + acetyl phosphate

642342

-

2.7.2.7

ATP + acetate = ADP + acetyl phosphate

-

-

4.1.2.22

D-Fructose 6-phosphate + phosphate = Acetyl phosphate + D-erythrose 4-phosphate + H2O

, 5095, 653088, 651682

-

4.1.2.22

D-fructose 6-phosphate + phosphate = acetyl phosphate + H2O + erythrose 4-phosphate

-

-

4.1.2.22

D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate

-

-

4.1.2.22

D-Xylulose 5-phosphate + phosphate = Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O

-

-

4.1.2.22

D-xylulose 5-phosphate + phosphate = acetyl phosphate + H2O + D-glyceraldehyde 3-phosphate

-

-

4.1.2.9

D-Fructose 6-phosphate + phosphate = Acetyl phosphate + D-erythrose 4-phosphate + H2O

-

-

4.1.2.9

D-ribulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O

-

-

4.1.2.9

D-xylulose 5-phosphate + phosphate = acetyl phosphate + D-glyceraldehyde 3-phosphate

, 650858, 649379, 651682

-

4.1.2.9

D-Xylulose 5-phosphate + phosphate = Acetyl phosphate + D-glyceraldehyde 3-phosphate + H2O

, 37325

-

4.1.2.9

D-xylulose 5-phosphate = pyruvate + acetyl phosphate

-

-

4.1.2.9

Ribulose 5-phosphate + phosphate = Acetyl phosphate + D-glyceraldehyde 3-phosphate

-

-

4.1.2.22

5 entries

4.1.2.9

6 entries

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.40

-

739641

-

1.2.7.6

stimulates

644692

-

2.3.1.304

10 mM acetyl phosphate activates both the native and the dephosphorylated enzyme 6fold and 2fold, respectively

761890

-

2.3.1.304

activates the enzyme and the level of activation is dependent on the concentration of acetyl phosphate supplementation

688122

-

2.3.1.304

2 entries

2.7.1.20

10 mM, activity is stimulated more than 10fold

675945

-

2.7.7.65

-

725263

-

Inhibitor in Enzyme-catalyzed Reactions (16 results)

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Show Inhibitors (16 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.40

slight inhibition at 2 mM

760644

-

1.13.11.72

-

719645

-

1.21.4.2

inhibits protein C activity, although a substrate

636472

-

2.1.3.2

-

485856

-

2.1.3.2

3 mM, 50% inhibition

485875

-

2.3.1.8

-

487535

1xco, 3D-view

2.3.1.8

substrate inhibition; substrate inhibition

720421

1xco, 3D-view

2.5.1.3

0.5 mM, 50% inhibition, uncompetitive with respect to both substrates

639722

-

2.5.1.3

4 mM, 82.8% inhibition

639723

-

2.7.2.1

-

642173, 642176

-

2.7.2.1

product inhibition

642197

-

2.7.2.1

product inhibition is noncompetitive versus both acetate and ATP

642168

-

5.3.1.1

-

2561

-

5.3.1.1

competitive

2560

-

2.1.3.2

2 entries

2.3.1.8

2 entries

2.5.1.3

2 entries

2.7.2.1

3 entries

5.3.1.1

2 entries

6.2.1.B11

-

744820

-

6.3.4.3

inhibits ATP synthesis reaction from carbamoyl phosphate and ADP, and synthesis of 10-formyltetrahydrofolate

1508

-

3D Structure of Enzyme-Ligand-Complex (PDB) (7 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (7 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.1.8

1xco, 3D-view

5.4.2.6

6h91, 3D-view

5.4.2.6

6h92, 3D-view

5.4.2.6

6h91, 3D-view

5.4.2.6

6h92, 3D-view

5.4.2.6

6h91, 3D-view

5.4.2.6

6h92, 3D-view

5.4.2.6

6 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (71 results)

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Show Turnover Number (71 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.1.222

2.65

-

pH 7.4, 55°C

756682

2.3.1.222

5.4

-

reverse reaction, pH and temperature not specified in the publication

719708

2.3.1.8

0.15

-

mutant Pta-F1, pH 8.0, 30°C

719451

2.3.1.8

1.32

-

C159A mutant

487542

2.3.1.8

1.56

-

mutant Pta-F1, pH 8.0, 30°C

719451

2.3.1.8

1.63

-

R310Q mutant

487542

2.3.1.8

2.16

-

mutant Pta-F1, pH 8.0, 30°C

719451

2.3.1.8

2.65

-

pH 7.6, 55°C

756682

2.3.1.8

3.03

-

C159A/C277A/C312A/C325A mutant

487542

2.3.1.8

4.93

-

R87Q mutant

487542

2.3.1.8

5.45

-

mutant R287Q

487542

2.3.1.8

12.5

-

R133Q mutant

487542

2.3.1.8

24.1

-

mutant R28Q

487542

2.3.1.8

40.6

-

wild type

487542

2.3.1.8

44.5

-

C312A mutant

487542

2.3.1.8

51.6

-

C277A/C312A/C325A mutant

487542

2.3.1.8

57.6

-

C325A mutant

487542

2.3.1.8

66.3

-

C159S mutant

487542

2.3.1.8

68.5

-

wild-type after expression in E. coli

487542

2.3.1.8

94.9

-

C277A mutant

487542

2.3.1.8

227

-

wild-type, pH 8.0, 30°C

719451

2.3.1.8

403.5

-

mutant enzyme M294I

674792

2.3.1.8

415

-

pH 7.8, 30°C

720217

2.3.1.8

574.5

-

wild-type enzyme

674792

2.3.1.8

1301

-

mutant enzyme G273D

674792

2.3.1.8

1480

-

mutant enzyme R252H

674792

2.3.1.8

1500

-

25°C, pH 7.2

674263

2.3.1.8

1927

-

30°C, calculated per monomer

659038

2.3.1.8

5190

-

25°C, pH 7.2

674263

2.7.2.1

12

-

mutant enzyme G331Q/I332M, at pH 7.0 and 37°C

762441

2.7.2.1

12

-

mutant F179A, pH 7.4

659065

2.7.2.1

93

-

pH 7.5, 30°C, recombinant His-tagged isozyme AckA2

738528

2.7.2.1

105

-

at pH 8.0 and 37°C

757471

2.7.2.1

316.7

-

pH 8.0, 30°C

746769

2.7.2.1

700

-

pH 7.0, 36°C

642187

2.7.2.1

875

-

pH 7.4, 25°C

642176

2.7.2.1

875

-

pH 7.5, 10°C, recombinant enzyme

739591

2.7.2.1

890

-

pH 7.5, 10°C, recombinant enzyme

739591

2.7.2.1

1039

-

mutant L122A, pH 7.4

659065

2.7.2.1

1105

-

pH 7.5, 30°C, recombinant His-tagged isozyme AckA1

738528

2.7.2.1

1340

-

pH 7.5, 15°C, recombinant enzyme

739591

2.7.2.1

1550

-

pH 7.5, 15°C, recombinant enzyme

739591

2.7.2.1

1550

-

wild type enzyme, at pH 7.0 and 37°C

762441

2.7.2.1

1700

-

pH 7.5, 20°C, recombinant enzyme

739591

2.7.2.1

1764

-

pH 7.5, 37°C

721949

2.7.2.1

2100

-

pH 7.5, 25°C, recombinant enzyme

739591

2.7.2.1

2150

-

pH 7.5, 20°C, recombinant enzyme

739591

2.7.2.1

2396

-

mutant P232A, pH 7.4

659065

2.7.2.1

2572

-

mutant V93G, pH 7.4

659065

2.7.2.1

2680

-

wild-type, pH 7.4

659065

2.7.2.1

3167

-

pH 8.0, 30°C

737465

2.7.2.1

3600

-

pH 7.5, 25°C, recombinant enzyme

739591

2.7.2.1

3869

-

mutant V93A, pH 7.4

659065

2.7.2.12

0.052

-

mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C

762441

2.7.2.12

2

-

37°C, pH 7, mutant H172A

722150

2.7.2.12

14

-

mutant enzyme Q323A/M324A, at pH 7.0 and 37°C

762441

2.7.2.12

21

-

37°C, pH 7, mutant H117A

722150

2.7.2.12

21

-

at pH 6.0 and 37°C

744414

2.7.2.12

21

-

pH 6.0, 37°C, recombinant enzyme

737773

2.7.2.12

30

-

at pH 7.0 and 37°C

744414

2.7.2.12

30

-

pH 7.0, 37°C, recombinant enzyme

737773

2.7.2.12

32

-

mutant enzyme Q323G/M324I, at pH 7.0 and 37°C

762441

2.7.2.12

97

-

37°C, pH 7, mutant V87G

722150

2.7.2.12

266

-

wild type enzyme, at pH 7.0 and 37°C

762441

2.7.2.12

280

-

37°C, pH 7, mutant I116A

722150

2.7.2.12

344

-

37°C, pH 7, mutant I116L

722150

2.7.2.12

1218

-

37°C, pH 7, mutant V87A

722150

2.7.2.12

1939

-

37°C, pH 7, wild-type

722150

2.7.2.12

8333

-

37°C, pH 7, mutant T223P

722150

3.6.1.7

0.00000155

-

wild type enzyme, pH and temperature not specified in the publication

734482

3.6.1.7

0.043

-

mutant enzyme C20R, pH and temperature not specified in the publication

734482

2.3.1.222

2 entries

2.3.1.8

27 entries

2.7.2.1

24 entries

2.7.2.12

16 entries

3.6.1.7

2 entries

K_M Value (121 results)

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Show KM Value (121 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.222

0.4

-

pH 7.4, 55°C

756682

2.3.1.222

0.97

-

reverse reaction, pH and temperature not specified in the publication

719708

2.3.1.32

1.35

-

cosubstrate L-ornithine

486790

2.3.1.32

12.4

-

cosubstrate L-lysine

486790

2.3.1.8

0.024

-

-

487537

2.3.1.8

0.043

-

R87Q mutant

487542

2.3.1.8

0.073

-

R133Q mutant

487542

2.3.1.8

0.094

-

23°C, pH 7.2, mutant enzyme S309A

674262

2.3.1.8

0.096

-

25°C, pH 7.2

674263

2.3.1.8

0.129

-

30°C

659038

2.3.1.8

0.143

-

23°C, pH 7.2, mutant enzyme D316E

674262

2.3.1.8

0.166

-

R287Q mutant

487542

2.3.1.8

0.17

-

wild tpye

487542

2.3.1.8

0.175

-

23°C, pH 7.2, mutant enzyme S309T

674262

2.3.1.8

0.18

-

wild-type after expression in E. coli

487542

2.3.1.8

0.185

-

23°C, pH 7.2, wild-type enzyme

674262

2.3.1.8

0.186

-

25°C, pH 7.2

674263

2.3.1.8

0.187

-

C277A mutant

487542

2.3.1.8

0.191

-

C159S mutant

487542

2.3.1.8

0.198

-

C312A mutant

487542

2.3.1.8

0.206

-

C159A mutant

487542

2.3.1.8

0.222

-

C159A/C277A/C312A/C325A mutant

487542

2.3.1.8

0.23

-

C325A mutant

487542

2.3.1.8

0.254

-

C277A/C312A/C325A mutant

487542

2.3.1.8

0.255

-

23°C, pH 7.2, mutant enzyme S309C

674262

2.3.1.8

0.311

-

-

487517

2.3.1.8

0.312

-

pH 7.8, 30°C

720217

2.3.1.8

0.4

-

pH 7.6, 55°C

756682

2.3.1.8

0.464

-

pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB

720425

2.3.1.8

0.5

-

pH 7.2, 35°C

720421

2.3.1.8

0.531

-

23°C, pH 7.2, mutant enzyme R310K

674262

2.3.1.8

0.59

-

-

487522

2.3.1.8

0.616

-

pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB

720425

2.3.1.8

0.66

-

-

487514, 487517

2.3.1.8

0.775

-

23°C, pH 7.2, mutant enzyme R310Q

674262

2.3.1.8

0.775

-

R310Q mutant

487542

2.3.1.8

0.9

-

wild-type, pH 8.0, 30°C

719451

2.3.1.8

1

-

pH 7.2, 35°C

720421

2.3.1.8

1.1

-

mutant Pta-F1, pH 8.0, 30°C

719451

2.3.1.8

1.3

-

-

487540

2.3.1.8

1.32

-

R28Q mutant

487542

2.3.1.8

1.7

-

mutant Pta-F1, pH 8.0, 30°C

719451

2.3.1.8

2.4

-

mutant Pta-F1, pH 8.0, 30°C

719451

2.3.1.8

4.7

-

-

487525

2.3.1.8

22.5

-

23°C, pH 7.2, mutant enzyme R310A

674262

2.3.1.222

2 entries

2.3.1.32

2 entries

2.3.1.8

41 entries

2.7.1.146

11.9

-

pH 6.5, 50°C

395269

2.7.1.61

0.4

-

carbamoyl phosphate, D-mannose 6-phosphate, pH 7.5, 25°C

636972, 636973

2.7.2.1

0.0026

-

carried out at various temperatures

642183

2.7.2.1

0.0222

-

at pH 8.0 and 37°C

757471

2.7.2.1

0.1

-

pH 7.4, 25°C

642176

2.7.2.1

0.11

-

pH 8.0, 30°C

737465, 746769

2.7.2.1

0.15

-

mutant F179A, pH 7.4

659065

2.7.2.1

0.16

-

-

642182

2.7.2.1

0.16

-

pH 7.9, 37°C

642182

2.7.2.1

0.2

-

pH 7.4, 25°C, 0.5 M NaCl

642176

2.7.2.1

0.26

-

Q43W

690888

2.7.2.1

0.28

-

pH 7.5, 37°C

721949

2.7.2.1

0.33

-

R241/Q43W

690888

2.7.2.1

0.34

-

wild-type, pH 7.4

659065

2.7.2.1

0.44

-

pH 7.0, 50°C

487537

2.7.2.1

0.44

-

pH 7.5, 30°C

642181

2.7.2.1

0.47

-

wild-type

690888

2.7.2.1

0.47

-

wild-type, pH 7.4

659446

2.7.2.1

0.5

-

mutant L122A, pH 7.4

659065

2.7.2.1

0.5

-

pH 7.5, 25°C, recombinant enzyme

739591

2.7.2.1

0.53

-

pH 7.5, 10°C, recombinant enzyme

739591

2.7.2.1

0.53

-

pH 7.5, 15°C, recombinant enzyme

739591

2.7.2.1

0.53

-

pH 7.5, 20°C, recombinant enzyme

739591

2.7.2.1

0.54

-

pH 7.5, 30°C, recombinant His-tagged isozyme AckA1

738528

2.7.2.1

0.55

-

pH 7.5, 30°C, recombinant His-tagged isozyme AckA2

738528

2.7.2.1

0.58

-

pH 7.3, 30°C

642189

2.7.2.1

0.59

-

pH 7.5, 25°C, recombinant enzyme

739591

2.7.2.1

0.61

-

mutant R91K, pH 7.4

659446

2.7.2.1

0.67

-

pH 7.5, 20°C, recombinant enzyme

739591

2.7.2.1

0.69

-

pH 7.5, 10°C, recombinant enzyme

739591

2.7.2.1

0.71

-

mutant V93G, pH 7.4

659065

2.7.2.1

0.71

-

pH 7.5, 15°C, recombinant enzyme

739591

2.7.2.1

0.74

-

mutant V93A, pH 7.4

659065

2.7.2.1

0.84

-

mutant R241A, pH 7.4

659446

2.7.2.1

0.92

-

mutant R241K, pH 7.4

659446

2.7.2.1

1

-

pH 7.5, 30°C

642195

2.7.2.1

1.02

-

R241K/Q43W

690888

2.7.2.1

1.08

-

R91K/Q43W

690888

2.7.2.1

1.19

-

mutant P232A, pH 7.4

659065

2.7.2.1

1.2

-

pH 7.4, 37°C

642173

2.7.2.1

1.2

-

wild type enzyme, at pH 7.0 and 37°C

762441

2.7.2.1

1.36

-

mutant R91A, pH 7.4

659446

2.7.2.1

1.64

-

mutant R241L, pH 7.4

659446

2.7.2.1

1.7

-

mutant enzyme G331Q/I332M, at pH 7.0 and 37°C

762441

2.7.2.1

2.3

-

mutant R91L, pH 7.4

659446

2.7.2.1

2.58

-

R91A/Q43W

690888

2.7.2.1

3.3

-

pH 7.3, 37°C, 2.0 M succinate

642171

2.7.2.1

5

-

pH 7.3, 37°C, 0.2 M succinate

642171

2.7.2.1

5

-

pH 7.4

642166

2.7.2.1

7

-

pH 7.3, 37°C

642175

2.7.2.12

0.02

-

at pH 6.0 and 37°C

744414

2.7.2.12

0.02

-

pH 7.0, 37°C, recombinant enzyme

737773

2.7.2.12

0.06

-

pH 7, 30°C

642212

2.7.2.12

0.07

-

at pH 6.0 and 37°C

744414

2.7.2.12

0.07

-

pH 6.0, 37°C, recombinant enzyme

737773

2.7.2.12

0.34

-

mutant enzyme Q323A/M324A, at pH 7.0 and 37°C

762441

2.7.2.12

0.47

-

mutant enzyme Q323G/M324I, at pH 7.0 and 37°C

762441

2.7.2.12

0.5

-

37°C, pH 7, wild-type

722150

2.7.2.12

0.51

-

37°C, pH 7, mutant V87G

722150

2.7.2.12

0.53

-

37°C, pH 7, mutant V87A

722150

2.7.2.12

0.57

-

wild type enzyme, at pH 7.0 and 37°C

762441

2.7.2.12

0.66

-

mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37°C

762441

2.7.2.12

0.69

-

37°C, pH 7, mutant H172A

722150

2.7.2.12

1.6

-

37°C, pH 7, mutant I116A

722150

2.7.2.12

2

-

37°C, pH 7, mutant T223P

722150

2.7.2.12

2.4

-

37°C, pH 7, mutant I116L

722150

2.7.2.12

8

-

37°C, pH 7, mutant H117A

722150

3.6.1.7

1.08

-

GP1

246778

3.6.1.7

2.36

-

mutant enzyme C20R, pH and temperature not specified in the publication

734482

3.6.1.7

2.9

-

erythrocyte enzyme

246775, 246800

3.6.1.7

4.23

-

erythrocyte enzyme

246792

3.6.1.7

6.2

-

skeletal muscle enzyme

246775, 246800

3.6.1.7

8.53

-

wild type enzyme, pH and temperature not specified in the publication

734482

2.7.2.1

48 entries

2.7.2.12

17 entries

3.6.1.7

6 entries

6.3.1.21

0.48

-

recombinant enzyme, pH 8.0, 25°C, reaction with ADP

760556

7.6.2.1

1.03

-

phosphatase activity

246837

7.6.2.1

1.31

-

phosphatidylserine translocase activity

246837

7.6.2.1

2 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.8

5.2

-

pH 7.2, 35°C

720421

2.3.1.8

12

-

pH 7.2, 35°C

720421

2.3.1.8

2 entries

References & Links

Literature References (171)

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Show Reference (171 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1508

444533

Carbamyl phosphate-dependent ATP synthesis catalyzed by formyltetrahydrofolate synthetase

1979

Buttlaire, D.H.; Balfe, C.A.; Wendland, M.F.; Himes, R.H.

Biochim. Biophys. Acta

567

453-463

2560

-

Triosephosphate isomerase from yeast

1975

Krietsch, W.K.G.

Methods Enzymol.

41B

434-438

2561

-

Triosephosphate isomerase from rabbit liver

1975

Krietsch, W.K.G.

Methods Enzymol.

41B

438-442

5095

13610828

Phosphorolytic cleavage of fructose-6-phosphate by fructose-6-phosphate phosphoketolase from Acetobacter xylinum

1958

Schramm, M.; Klybas, V.; Racker, E.

J. Biol. Chem.

233

1283-1288

37325

-

A novel pathway of glucose catabolism in Thiobacillus novellus

1979

Greenley, D.E.; Smith, D.W.

Arch. Microbiol.

122

257-261

94495

16347818

Acetate-activating enzymes of Bradyrhizobium japonicum bacteroids

1989

Preston, G.G.; Zeiher, C.; Wall, J.D.; Emerich, D.W.

Appl. Environ. Microbiol.

55

165-170

114312

8069629

A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase

1993

Muller, Y.A.; Lindqvist, Y.; Furey, W.; Schulz, G.E.; Jordan, F.; Schneider, G.

Structure

1

95-103

134766

4235424

Properties of an acid phosphatase in Escherichia coli

1968

Hafkenscheid, J.C.M.

Biochim. Biophys. Acta

167

582-589

134772

14460641

Purification and properties of an acid phosphomonoesterase from Neurospora crassa

1961

Kuo, M.H.; Blumenthal, H.J.

Biochim. Biophys. Acta

52

13-29

246775

3026468

A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure

1986

Liguri, G.; Camici, G.; Manao, G.; Cappugi, G.; Nassi, P.; Modesti, A.; Ramponi, G.

Biochemistry

25

8089-8094

246778

6320809

Studies on synthesis and degradation rates and some molecular properties of guinea-pig muscle acylphosphatase

1984

Liguri, G.; Nassi, P.; Camici, G.; Manao, G.; Cappugi, G.; Stefani, M.; Berti, A.; Ramponi, G.

Biochem. J.

217

499-505

246781

237200

1,3-Diphosphoglycerate phosphatase

1975

Ramponi, G.

Methods Enzymol.

42C

409-426

246784

4344156

Purification and some molecular properties of horse liver acyl phosphatase

1972

Ramponi, G.; Nassi, P.; Cappugi, G.; Treves, C.; Manao, G.

Biochim. Biophys. Acta

284

485-496

246785

4313603

Isolation and crystallization of acyl phosphatase from rabbit muscle

1970

Shiokawa, H.; Noda, L.

J. Biol. Chem.

245

669-673

246786

4305161

Horse muscle acyl phosphatase: purification and some properties

1969

Ramponi, G.; Guerritore, A.; Treves, C.; Nassi, P.; Baccari, V.

Arch. Biochem. Biophys.

130

362-369

246787

14435883

Further purification and properties of brain acyl phosphatase

1960

Raijman, L.; Grisolia, S.; Edelhoch, H.

J. Biol. Chem.

235

2340-2342

246792

8262761

Purification, kinetic properties and primary structure of bovine erythrocyte acylphosphatase

1993

Pazzagli, L.; Ikram, U.K.; Liguri, G.; Taddei, N.; Gentilini, A.; Cecchi, C.; Manao, G.; Cappugi, G.

Ital. J. Biochem.

42

233-245

246795

7720867

Properties of N-terminus truncated and C-terminus mutated muscle acylphosphatases

1995

Taddei, N.; Modesti, A.; Bucciantini, M.; Stefani, M.; Magherini, F.; Vecchi, M.; Raugei, G.; Ramponi, G.

FEBS Lett.

362

175-179

246799

9477974

Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH

1998

Chiti, F.; van Nuland, N.A.J.; Taddei, N.; Magherini, F.; Stefani, M.; Ramponi, G.; Dobson, C.M.

Biochemistry

37

1447-1455

246800

-

Acylphosphate phosphohydrolases

1995

Stefani, M.; Ramponi, G.

Life Chem. Rep.

12

271-301

246837

9030722

Characterization of the correlation between ATP-dependent aminophospholipid translocation and Mg2+-ATPase activity in red blood cell membranes

1997

Beleznay, Z.; Zachowski, A.; Devaux, P.F.; Ott, P.

Eur. J. Biochem.

243

58-65

390429

10978159

Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum

2000

Tittmann, K.; Golbik, R.; Ghisla, S.; Hubner, G.

Biochemistry

39

10747-10754

390430

9582325

Activation of thiamin diphosphate and FAD in the phosphate-dependent pyruvate oxidase from Lactobacillus plantarum

1998

Tittmann, K.; Proske, D.; Spinka, M.; Ghisla, S.; Rudolph, R.; Hubner, G.; Kern, G.

J. Biol. Chem.

273

12929-12934

390431

-

Phosphate sensing system using pyruvate oxidase and chemiluminescence detection

1996

Ikebukuro, K.; Wakamura, H.; Karube, I.

Biosens. Bioelectron.

11

959-965

390432

8820650

Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae

1996

Spellerberg, B.; Cundell, D.R.; Sandros, J.; Pearce, B.J.; Idänpään-Heikkilä, I.; Rosenow, C.; Masure, H.R.

Mol. Microbiol.

19

803-813

390433

8145244

The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum

1994

Muller, Y.A.; Schumacher, G.; Rudolph, R.; Schulz, G.E.

J. Mol. Biol.

237

315-335

390435

-

Pyruvate oxidase activity dependent on thiamine pyrophosphate, flavin adenine dinucleotide and orthophosphate in Streptococcus sanguis

1985

Carlsson, J.; Kujala, U.

FEMS Microbiol. Lett.

25

53-56

390436

6480562

Physiological role of pyruvate oxidase on the aerobic metabolism of Lactobacillus plantarum

1984

Sedewitz, B.; Schleifer, K.H.; Götz, F.

J. Bacteriol.

160

462-465

390437

6480556

Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum

1984

Sedewitz, B.; Schleifer, K.H.; Götz, F.

J. Bacteriol.

160

273-278

395269

11717273

ADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea

2001

Verhees, C.H.; Tuininga, J.E.; Kengen, S.W.; Stams, A.J.; van der Oost, J.; de Vos, W.M.

J. Bacteriol.

183

7145-7153

484935

11422384

In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue

2001

Bednarski, B.; Andreesen, J.R.; Pich, A.

Eur. J. Biochem.

268

3538-3544

485856

-

Plant aspartate transcarbamylase: kinetic properies of the enzyme from mung bean (Phaseolus aureus) seedlings

1978

Savithri, H.S.; Vaidyanathan, C.S.; Rao, N.A.

Proc. Indian Acad. Sci. Sect. B

87B

81-94

485875

9344472

In situ properties of Helicobacter pylori aspartate carbamoyltransferase

1997

Burns, B.P.; Mendz, G.L.; Hazell, S.L.

Arch. Biochem. Biophys.

347

119-125

486790

14240571

Enzyme synthesis of epsilon-N-acetyl-L-lysine

1964

Paik, W.K.; Kim, S.

Arch. Biochem. Biophys.

108

221-229

487218

4340563

Properties and function of the pyruvate-formate-lyase reaction in clostridiae

1972

Thauer, R.K.; Kirchniawy, F.H.; Jungermann, K.A.

Eur. J. Biochem.

27

282-290

487513

-

Phosphotransacetylase from Clostridium kluyveri

1955

Stadtman, E.R.

Methods Enzymol.

1

596-599

487514

14087284

Phosphotransacetylase aus Clostridium kluyveri

1963

Bergmeyer, H.U.; Holz, G.; Klotsch, H.; Lang, G.

Biochem. Z.

338

114-121

487515

12980995

The purification and properties of phosphotransacetylase

1952

Stadtman, E.R.

J. Biol. Chem.

196

527-534

487516

6639958

Irreversible inhibition of phosphotransacetylase by S-dimethylarsino-CoA

1983

Duhr, E.F.; Owens, M.S.; Barden, R.E.

Biochim. Biophys. Acta

749

84-90

487517

-

Purification and properties of phosphotransacetylase from the eucaryotic green alga Chlorogonium elongatum

1985

Kreuzberg, K.; Umlauf, H.; Blaschkowski, H.P.

Biochim. Biophys. Acta

842

22-29

487518

952869

Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase

1976

Henkin, J.; Abeles, R.H.

Biochemistry

15

3472-3479

487519

4750760

Kinetic studies with phosphotransacetylase. V. The mechanism of activation by univalent cations

1973

Kyrtopoulos, S.A.; Satchell, D.P.N.

Biochim. Biophys. Acta

321

126-142

487520

5026307

Kinetic studies with phosphotransacetylase. II. The acetylation of arsenate by acetyl coenzyme A

1972

Kyrtopoulos, S.A.; Satchell, D.P.N.

Biochim. Biophys. Acta

268

334-343

487521

5121614

Kinetic studies with phosphotransacetylase

1971

Hibbert, F.; Kyrtopoulos, S.A.; Satchell, D.P.N.

Biochim. Biophys. Acta

242

39-54

487522

4360222

Kinetic properties of phosphotransacetylase from Veillonella alcalescens

1972

Pelroy, R.A.; Whiteley, H.R.

J. Bacteriol.

111

47-55

487523

5012766

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