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  • In Vivo Product
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Ligand 3-phospho-D-glyceroyl phosphate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

glycolysis, photosynthesis

KEGG

Biosynthesis of alkaloids derived from shikimate pathway, Biosynthesis of amino acids, Biosynthesis of antibiotics, Biosynthesis of phenylpropanoids, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of terpenoids and steroids, Carbon fixation in photosynthetic organisms, Carbon metabolism, Glycolysis / Gluconeogenesis, Microbial metabolism in diverse environments more

MetaCyc

1-butanol autotrophic biosynthesis (engineered), Bifidobacterium shunt, Calvin-Benson-Bassham cycle, Entner-Doudoroff pathway I, formaldehyde assimilation III (dihydroxyacetone cycle), gluconeogenesis I, gluconeogenesis III, glycerol degradation to butanol, glycolysis I (from glucose 6-phosphate), glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), glycolysis IV (plant cytosol), heterolactic fermentation, Rapoport-Luebering glycolytic shunt, sucrose biosynthesis I (from photosynthesis), superpathway of glucose and xylose degradation, zwittermicin A biosynthesis more

Show all BRENDA pathways known for 3-phospho-D-glyceroyl phosphate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Natural Substrate (13 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.12

3-phospho-D-glyceroyl phosphate + NADH = D-glyceraldehyde 3-phosphate + phosphate + NAD+

287915

-

1.2.1.12

3-phospho-D-glyceroyl phosphate + NADH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NAD+

673587, 676334, 663144, 726190

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH = D-glyceraldehyde 3-phosphate + phosphate + NADP+

287973, 288034, 287990, 288004

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+

673549, 724306, 671401, 676575

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH + H+ = DL-glyceraldehyde 3-phosphate + phosphate + NADP+

725013

-

1.2.1.12

2 entries

1.2.1.13

3 entries

1.2.1.59

3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+

725013

-

1.2.1.9

3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+

673549, 676575

-

2.7.1.106

3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate = 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate

640349, 640348

-

2.7.2.10

GDP + 3-phospho-D-glyceroyl 1-phosphate = GTP + 3-phospho-D-glycerate

645109

-

2.7.2.3

ADP + 3-phospho-D-glyceroyl phosphate = ATP + 3-phospho-D-glycerate

642242, 642274, 642293, 642294, 642292, 642303, 642281, 642286, 642236, 642251, 642252, 642238

2x15, 3D-view

2.7.4.17

1,3-diphosphoglyceric acid + (polyphosphate)n = 3-phosphoglycerate + (polyphosphate)n+1

642547

-

3.6.1.7

1,3-diphosphoglycerate + H2O = 3-phosphoglycerate + phosphate

246772, 246800, 246784, 246781

-

5.4.2.4

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate

706143, 660653, 662264, 728236, 728437, 748733, 651748

-

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

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.12

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.13

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.59

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.59

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.12

2 entries

1.2.1.13

3 entries

1.2.1.59

2 entries

1.2.1.9

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

2.7.2.3

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

Substrate in Enzyme-catalyzed Reactions (30 results)

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Show Substrate (30 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.12

3-phospho-D-glyceroyl phosphate + NADH = D-glyceraldehyde 3-phosphate + phosphate + NAD+

287932, 287900, 287913, 287934, 287899, 287931, 287937, 287979, 287933, 287946, 287973, 287909, 287936, 287906, 287930, 726190, 724415, 287915

-

1.2.1.12

3-phospho-D-glyceroyl phosphate + NADH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NAD+

673587, 676334, 663144, 743402, 726190

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADH = D-glyceraldehyde 3-phosphate + phosphate + NAD+

655452, 655492, 656539

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH = D-glyceraldehyde 3-phosphate + phosphate + NADP+

288008, 655452, 655492, 287990, 656539, 724415, 287992, 287973, 288034, 288004

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NAD+

724306

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+

673549, 724306, 671401, 676575

-

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH + H+ = DL-glyceraldehyde 3-phosphate + phosphate + NADP+

725013

-

1.2.1.12

2 entries

1.2.1.13

5 entries

1.2.1.59

3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+

725013

-

1.2.1.9

3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+

673549, 676575

-

2.7.1.106

3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate = 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate

640349, 640350, 640348

-

2.7.1.106

3-phospho-D-glyceroyl phosphate + D-mannose 1-phosphate = 3-phospho-D-glycerate + D-mannose 1,6-bisphosphate

640349, 640348

-

2.7.1.106

3-phospho-D-glyceroyl phosphate + D-glucose 6-phosphate = 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate

640349, 640348

-

2.7.1.106

3 entries

2.7.2.10

GDP + 3-phospho-D-glyceroyl 1-phosphate = GTP + 3-phospho-D-glycerate

703640, 645109

-

2.7.2.3

ADP + 3-phospho-D-glyceroyl phosphate = ATP + 3-phospho-D-glycerate

642242, 681295, 686757, 689257, 642274, 678829, 642293, 642294, 642292, 642303, 642281, 722701, 642286, 642236, 642251, 642252, 642238, 677941, 685259, 685273, 685227

2x15, 3D-view

2.7.2.3

L-ADP + 3-phospho-D-glyceroyl phosphate = ATP + 3-phospho-D-glycerate

684894

2x15, 3D-view

2.7.2.3

ADP + 3-phospho-D-glyceroyl 1-phosphate = 3-phospho-D-glycerate

702329, 703640, 706637, 705178

2x15, 3D-view

2.7.2.3

ADP + 3-phospho-D-glyceroyl 1-phosphate = ATP + 3-phospho-D-glycerate

703640

2x15, 3D-view

2.7.2.3

ADP + 1,3-bisphosphoglycerate = ATP + 3-phosphoglycerate

722979

2x15, 3D-view

2.7.2.3

D-ADP + 1,3-bisphosphoglycerate = ?

722979

2x15, 3D-view

2.7.2.3

D-ATP + 1,3-bisphospho-D-glycerate = ?

721425

2x15, 3D-view

2.7.2.3

D-CDP + 1,3-bisphospho-D-glycerate = ?

721425

2x15, 3D-view

2.7.2.3

L-ADP + 1,3-bisphosphoglycerate = ?

722979

2x15, 3D-view

2.7.2.3

L-ATP + 1,3-bisphospho-D-glycerate = ?

721425

2x15, 3D-view

2.7.2.3

L-CDP + 1,3-bisphospho-D-glycerate = ?

721425

2x15, 3D-view

2.7.2.3

11 entries

2.7.4.17

1,3-diphosphoglyceric acid + (polyphosphate)n = 3-phosphoglycerate + (polyphosphate)n+1

642547

-

3.6.1.7

1,3-diphosphoglycerate + H2O = 3-phosphoglycerate + phosphate

246772, 246776, 246781, 246800, 246789, 246797, 246775, 246791, 246794, 246795, 246796, 246799, 667099, 246790, 246792, 246793, 246782, 246784, 246786, 667089, 654097, 654100, 667658

-

3.6.1.7

1,3-bisphosphoglycerate + H2O = 3-phosphoglycerate + phosphate

654098

-

3.6.1.7

2 entries

5.4.2.2

Glucose 1-phosphate + 1,3-bisphosphoglycerate = Glucose 1,6-diphosphate + glycerate 3-phosphate

3284

-

5.4.2.4

1,3-Diphosphoglycerate = 2,3-Diphosphoglycerate

3313, 3314, 3319, 3320, 3257, 3324, 3323, 713630, 3318, 3251, 3306, 3307, 3308, 3309, 3310, 3326

-

5.4.2.4

3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate

706143, 651748, 660653, 662264, 728236, 728437, 748733

-

5.4.2.4

2 entries

Product in Enzyme-catalyzed Reactions (58 results)

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Show Product (58 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.12

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH

287967, 11542, 287949, 287924, 287946, 287980, 287957, 287958, 287982, 287926, 287938, 287968, 287927, 287977, 287983, 287910, 287925, 287945, 287950, 287900, 287913, 287932, 287929, 287960, 3246, 287914, 287966, 287934, 287899, 287943, 287948, 287952, 287954, 287975, 288344, 287931, 287937, 287905, 287911, 287979, 3247, 287953, 287959, 287965, 287969, 287972, 287978, 287981, 287933, 287973, 287917, 287947, 287962, 287970, 287984, 287985, 287909, 287903, 287915, 287902, 287935, 287961, 287936, 287920, 287919, 287901, 287907, 287974, 287918, 287928, 287912, 287944, 287963, 287971, 287976, 287922, 287956, 287986, 3241, 287916, 287906, 287923, 287908, 287987, 287930, 287942, 287951, 287964, 287904

-

1.2.1.12

D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate = 3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + poly(ethylene glycol)-bound NAD+ + phosphate = 3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate = 3-phospho-D-glyceroyl phosphate + ?

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + N6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+ + phosphate = 3-phospho-D-glyceroyl phosphate + N6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl)-NADH

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + C8-(4-(2,2,6,6-tetramethyl-piperidinyl-l-oxyl)-amino)-NAD+ + phosphate = 3-phospho-D-glyceroyl phosphate + C8-(4-(2,2,6,6-tetramethyl-piperidinyl-l-oxyl)-amino)-NADH

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate = 3-phospho-D-glyceroyl phosphate + thio-NADH

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate = 3-phospho-D-glyceroyl phosphate + ?

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.12

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.13

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH

288024, 288027, 288022, 288032, 287999, 11537, 11539

-

1.2.1.13

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH

288024, 288002, 288022, 288032, 287999, 11537, 287989, 11539, 287995

-

1.2.1.13

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.13

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.59

D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+ = 1,3-diphosphoglycerate + NAD(P)H

11538, 11539

-

1.2.1.59

D-glyceraldehyde-3-phosphate + phosphate + NADP+ = 1,3-diphosphoglycerate + NADPH

11538, 11539

-

1.2.1.59

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

-

-

1.2.1.59

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

1.2.1.12

10 entries

1.2.1.13

6 entries

1.2.1.59

4 entries

1.2.1.9

D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

-

-

2.7.2.10

GTP + 3-phospho-D-glycerate = GDP + 3-phospho-D-glyceroyl 1-phosphate

-

-

2.7.2.10

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl 1-phosphate

-

-

2.7.2.10

ITP + 3-phospho-D-glycerate = IDP + 3-phospho-D-glyceroyl 1-phosphate

-

-

2.7.2.3

ATP + 3-phospho-D-glycerate = ADP + 1,3-diphosphoglycerate

642265, 642271, 642253, 642256, 642268, 642304, 642242, 642260, 642235, 642261, 642274, 642275, 642277, 642278, 642283, 642295, 642300, 642305, 642240, 642279, 642252, 642258, 642289, 642298, 642301, 642168, 642241, 642243, 642245, 642246, 642247, 642248, 642249, 642255, 642259, 642282, 642293, 642294, 642299, 642269, 642270, 642244, 642267, 642263, 642262, 642251, 642291, 2572, 642237, 642286, 642288, 642290, 642292, 642238, 3241, 642287, 642303, 642254, 642236, 642281, 642239, 642264, 642284, 642296, 642302, 642297, 642266, 642285, 642276, 642280, 642257

2x15, 3D-view

2.7.2.3

ITP + 3-phospho-D-glycerate = IDP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

dITP + 3-phospho-D-glycerate = dIDP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

GTP + 3-phospho-D-glycerate = GDP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

dGTP + 3-phospho-D-glycerate = dGDP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

dATP + 3-phospho-D-glycerate = dADP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

UTP + 3-phospho-D-glycerate = UDP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

CTP + 3-phospho-D-glycerate = CDP + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate = 2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate = beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate = beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate = 2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate

-

2x15, 3D-view

2.7.2.3

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl 1-phosphate

-

2x15, 3D-view

2.7.2.3

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

2',3'-didehydro-2',3'-dideoxythymidine triphosphate + 3-phospho-D-glycerate = 2',3'-didehydro-2',3'-dideoxythymidine diphosphate + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

2',3'-dideoxy-GTP + 3-phospho-D-glycerate = 2',3'-dideoxy-GDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

3'-deoxy-3'-azidothymidine triphosphate + 3-phospho-D-glycerate = 3'-deoxy-3'-azidothymidine diphosphate + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

acyclovir triphosphate + 3-phospho-D-glycerate = acyclovir diphosphate + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

2'-dATP + 3-phospho-D-glycerate = 2'-dADP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

2'-dGTP + 3-phospho-D-glycerate = 2'-dGDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

2'-dTTP + 3-phospho-D-glycerate = 2'-dTDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

D-ATP + 3-phospho-D-glycerate = D-ADP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

D-CTP + 3-phospho-D-glycerate = D-CDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

D-GTP + 3-phospho-D-glycerate = D-GDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

UTP + 3-phospho-D-glycerate = UDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-2'-dATP + 3-phospho-D-glycerate = L-2'-dADP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-2'-dGTP + 3-phospho-D-glycerate = L-2'-dGDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-2'-dTTP + 3-phospho-D-glycerate = L-2'-dTDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-ATP + 3-phospho-D-glycerate = L-ADP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-CTP + 3-phospho-D-glycerate = L-CDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-GTP + 3-phospho-D-glycerate = L-GDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

L-UTP + 3-phospho-D-glycerate = L-UDP + 3-phospho-D-glyceroyl phosphate

-

2x15, 3D-view

2.7.2.3

3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl 1-phosphate

-

2x15, 3D-view

2.7.2.3

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

-

2x15, 3D-view

2.7.2.10

3 entries

2.7.2.3

34 entries

Activator in Enzyme-catalyzed Reactions (4 results)

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Show Activating Compound (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.13

stimulates

288001

-

1.2.1.13

the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate. The actual activation and aggregation state of the enzyme in chloroplasts in light is regulated by the concentration of 1,3-diphosphoglycerate as activator in the stroma and its actual activity by the availability of 1,3-diphosphoglycerate as substrate

288032

-

1.2.1.13

most effective on a molar basis in stimulating NADPH-activity of dark chloroplast extracts and purified enzyme

288030

-

1.2.1.13

3 entries

2.7.2.3

substrate activation

642275

2x15, 3D-view

Inhibitor in Enzyme-catalyzed Reactions (7 results)

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Show Inhibitors (7 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.12

-

287936

-

1.2.1.13

-

725013

-

1.2.1.59

-

725013

-

2.7.1.11

0.385 mM and 0.005 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition

640518

-

2.7.2.3

-

642252

2x15, 3D-view

4.2.3.3

-

137612

-

5.4.2.2

-

3284, 3285

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

2.7.2.3

2x15, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (22 results)

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Show Turnover Number (22 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.12

0.06

-

mutant enzyme F37L, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

0.08

-

mutant enzyme F37T, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

0.14

-

mutant enzyme F37G, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

73.56

-

wild type enzyme, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.13

40

-

pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADH

655452

1.2.1.13

88

-

pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADH

655452

1.2.1.13

223

-

pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADPH

655452

1.2.1.13

419

-

pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADPH

655452

2.7.2.3

0.78

-

mutant enzyme K125A

685259

2.7.2.3

5.25

-

mutant enzyme k219A

685259

2.7.2.3

6

-

mutant enzyme R38A

685259

2.7.2.3

23.2

-

mutant enzyme N336A

685259

2.7.2.3

84

-

mutant enzyme E343A

685259

2.7.2.3

250

-

mutant enzyme T393A

686757

2.7.2.3

675

-

mutant enzyme T375A

685259

2.7.2.3

1130

-

mutant enzyme E192A

686757

2.7.2.3

1170

-

mutant enzyme F165A

686757

2.7.2.3

2630

-

wild-type enzyme

686757

2.7.2.3

2633

-

wild-type enzyme

685259

5.4.2.4

3.6

-

4°C

3323

5.4.2.4

12.5

-

25°C

3323

5.4.2.4

23.4

-

37°C

3323

1.2.1.12

4 entries

1.2.1.13

4 entries

2.7.2.3

11 entries

5.4.2.4

3 entries

K_M Value (84 results)

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Show KM Value (84 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.12

0.002

-

enzyme form E6.8, pH 7

287913

1.2.1.12

0.01

-

enzyme form E6.6, pH 7

287913

1.2.1.12

0.012

-

enzyme form E8.5, pH 7

287913

1.2.1.12

0.018

-

enzyme form E9.0, pH 7

287913

1.2.1.12

0.032

-

enzyme form E9.0, pH 9

287913

1.2.1.12

0.034

-

-

287900

1.2.1.12

0.035

-

enzyme form E8.5, pH 9

287913

1.2.1.12

0.036

-

wild type enzyme, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

0.036

-

wild-type, pH 8.8, 25°C

726190

1.2.1.12

0.042

-

enzyme form E6.6, pH 9

287913

1.2.1.12

0.049

-

mutant enzyme F37L, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

0.049

-

mutant F36L, pH 8.8, 25°C

726190

1.2.1.12

0.051

-

mutant enzyme F37G, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

0.051

-

mutant F36G, pH 8.8, 25°C

726190

1.2.1.12

0.053

-

mutant enzyme F37T, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

726190

1.2.1.12

0.053

-

mutant F36T, pH 8.8, 25°C

726190

1.2.1.12

0.1

-

glyoxysomal enzyme

287900

1.2.1.12

0.13

-

-

287900

1.2.1.12

0.14

-

-

287900

1.2.1.12

0.14

-

cytosolic enzyme

287900

1.2.1.12

0.172

-

enzyme form E6.8, pH 9

287913

1.2.1.12

0.22

-

pH 8.0, 5°C, euthermic

743402

1.2.1.12

0.24

-

pH 8.0, 36°C, long torpor; pH 8.0, 5°C, euthermic

743402

1.2.1.12

0.28

-

pH 8.0, 36°C, long torpor

743402

1.2.1.12

0.47

-

-

287973

1.2.1.12

1.78

-

pH 8.6, temperature not specified in the publication

724415

1.2.1.13

0.00041

-

pH 6.5, 70°C

724980

1.2.1.13

0.01

-

mutant enzyme T33A/S188A, reaction with NADH

656539

1.2.1.13

0.012

-

mutant enzyme S188A, reaction with NADH; mutant enzyme T33A, reaction with NADH; mutant enzyme T33A/S188A, reaction with NADPH; native enzyme A3-GAPDH, reaction with NADH

656539

1.2.1.13

0.012

-

mutant B(E362Q)

676575

1.2.1.13

0.013

-

mutant enzyme S188A, reaction with NADPH

656539

1.2.1.13

0.015

-

native enzyme A3-GAPDH, reaction with NADPH

656539

1.2.1.13

0.015

-

GapA; GapB, analyzed under reducing conditions

676575

1.2.1.13

0.016

-

with NADH as cofactor, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate

288032

1.2.1.13

0.016

-

mutant B(R77A)

676575

1.2.1.13

0.018

-

mutant enzyme T33A, reaction with NADPH

656539

1.2.1.13

0.019

-

A(plusCTE) mutant, analyzed under oxidizing conditions

676575

1.2.1.13

0.02

-

with NADPH as coenzyme, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate

288032

1.2.1.13

0.02

-

AB-GAPDH, analyzed under reducing conditions; GapB, analyzed under oxidizing conditions

676575

1.2.1.13

0.021

-

A(plusCTE) mutant, analyzed under reducing conditions

676575

1.2.1.13

0.022

-

B(minCTE) mutant

676575

1.2.1.13

0.024

-

AB-GAPDH, analyzed under oxidizing conditions

676575

1.2.1.13

0.027

-

mutant B(188)A, analyzed under oxidizing conditions

676575

1.2.1.13

0.031

-

mutant B(188)A, analyzed under reducing conditions

676575

1.2.1.13

5.8

-

wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C

725013

1.2.1.12

26 entries

1.2.1.13

19 entries

1.2.1.59

5.8

-

pH 8.0, 60°C

725013

1.2.1.9

0.012

-

mutant B(E362Q)

676575

1.2.1.9

0.015

-

GapA; GapB, analyzed under reducing conditions

676575

1.2.1.9

0.016

-

mutant B(R77A)

676575

1.2.1.9

0.019

-

A(plusCTE) mutant, analyzed under oxidizing conditions

676575

1.2.1.9

0.02

-

AB-GAPDH, analyzed under reducing conditions; GapB, analyzed under oxidizing conditions

676575

1.2.1.9

0.021

-

A(plusCTE) mutant, analyzed under reducing conditions

676575

1.2.1.9

0.022

-

B(minCTE) mutant

676575

1.2.1.9

0.024

-

AB-GAPDH, analyzed under oxidizing conditions

676575

1.2.1.9

0.027

-

mutant B(188)A, analyzed under oxidizing conditions

676575

1.2.1.9

0.031

-

mutant B(188)A, analyzed under reducing conditions

676575

2.7.1.106

0.000087

-

23°C, pH 8, Mg2+-enzyme in brain

640350

2.7.1.106

0.000091

-

23°C, pH 8, Zn2+-enzyme in brain

640350

2.7.1.106

0.00023

-

25°C, pH 7.5, liver enzyme peak I

640349

2.7.1.106

0.00028

-

25°C, pH 7.5, liver enzyme peak II

640349

2.7.1.106

0.00045

-

25°C, pH 7.5, erythrocyte enzyme

640349

2.7.2.3

0.0005

-

wild-type enzyme

686757

2.7.2.3

0.0013

-

mutant enzyme E343A

685259

2.7.2.3

0.0022

-

mutant enzyme N336A

685259

2.7.2.3

0.003

-

mutant enzyme T375A

685259

2.7.2.3

0.0038

-

mutant enzyme K125A

685259

2.7.2.3

0.005

-

wild-type enzyme

685259

2.7.2.3

0.0077

-

mutant enzyme k219A

685259

2.7.2.3

0.0091

-

mutant enzyme E192A

686757

2.7.2.3

0.01

-

mutant enzyme T393A

686757

2.7.2.3

0.017

-

mutant enzyme F165A

686757

2.7.2.3

0.29

-

mutant enzyme R38A

685259

2.7.2.3

5.6

-

70°C, pH 6.5

724980

3.6.1.7

0.12

-

erythrocyte enzyme

246781

3.6.1.7

0.55

-

erythrocyte enzyme

246775

3.6.1.7

0.55

-

erythrocyte enzyme

246800

3.6.1.7

0.62

-

skeletal muscle enzyme

246775

3.6.1.7

0.62

-

skeletal muscle enzyme

246800

3.6.1.7

1.6

-

muscle

246781

5.4.2.4

0.0005

-

pH 7.5, low salt concentration

3320

5.4.2.4

0.0007

-

pH 7.8

3314

5.4.2.4

0.003

-

pH 7.2, 0.1 M KCl

3320

5.4.2.4

0.0031

-

pH 7.2

3314

5.4.2.4

0.0036

-

pH 6.8

3314

1.2.1.9

10 entries

2.7.1.106

5 entries

2.7.2.3

12 entries

3.6.1.7

6 entries

5.4.2.4

5 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

1.2.1.13

49.1

-

wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C

725013

1.2.1.59

49.1

-

pH 8.0, 60°C

725013

References & Links

Literature References (264)

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Show Reference (264 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2572

6489338

Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei

1984

Misset, O.; Opperdoes, F.R.

Eur. J. Biochem.

144

475-483

3241

3026343

Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. The five enzymes from glyceraldehyde-3-phosphate dehydrogenase through to pyruvate kinase

1986

Pawluk, A.; Scopes, R.K.; Griffiths-Smith, K.

Biochem. J.

238

275-281

3246

6296621

Simultaneous purification of glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and phosphoglycerate mutase from pig liver and muscle

1982

Kulbe, K.D.; Foellmer, H.; Fuchs, J.

Methods Enzymol.

90

498-511

3247

7154963

Purification of all glycolytic enzymes from one muscle extract

1982

Scopes, R.K.; Stoter, A.

Methods Enzymol.

90

479-490

3251

212268

Immunochemical and enzymatic properties of bisphosphoglyceromutase/phosphatase and phosphoglyceromutase from human erythrocytes

1978

Ikura, K.; Narita, H.; Sasaki, R.; Chiba, H.

Eur. J. Biochem.

89

23-31

3257

182494

Subunit structure and multifunctional properties of yeast phosphoglyceromutase

1976

Sasaki, R.; Utsumi, S.; Sugimoto, E.; Chiba, H.

Eur. J. Biochem.

66

523-533

3284

-

Multifunctional properties of beef liver phosphoglucomutase

1976

Hirose, M.; Ueda, M.; Chiba, H.

Agric. Biol. Chem.

40

2433-2439

3285

-

Purification and properties of beef liver phosphoglucomutase

1976

Chiba, H.; Ueda, M.; Hirose, M.

Agric. Biol. Chem.

40

2423-2431

3306

9162026

Critical Role of Human bisphosphoglycerate mutase Cys22 in the phosphatase activator-binding site

1997

Ravel, P.; Craescus, C.T.; Arous, N.; Rosa, J.; Garel, M.C.

J. Biol. Chem.

272

14045-14050

3307

2145041

Human bisphosphogycerate mutase expressed in E. coli: purification, characterization and structure studies

1990

Calcin, M.C.; Blouquit, Y.; Garel, M.C.; Cohen-Solal, M.; Rosa, J.; Rosa, R.

Biochimie

72

337-343

3308

-

Natural and artificial mutants of the human 2,3-bisphosphoglycerate as a tool for the evaluation of structure-function relationship

1990

Garel, M.C.; Lemarchandel, M.O.; Prehu, M.O.; Calvin, M.C.; Arous, N.; Rosa, R.; Rosa, J.

Biomed. Biochim. Acta

49

166-171

3309

2553728

Human bisphosphglycerate mutase. Expression in Escherichia coli and use of site-directed mutagenesis in the evaluation of the role of the carboxyl-terminal region in the enzymatic mechanism

1989

Garel, M.C.; Joulin, V.; Le Boulch, P.; Calvin, M.C.; Prehu, M.O.; Arous, N.; Longin, R.; Rosa, R.; Rosa, J.; Cohen-Solal, M.

J. Biol. Chem.

264

18966-18972

3310

2542247

Isolation, characterization, and structure of a mutant 89 ARG->Cys bisphosphoglycerate mutase. Implication of the active site in the mutation

1989

Rosa, R.; Blouquit, Y.; Calvin, M.C.; Prome, D.; Prome, J.C.; Rosa, J.

J. Biol. Chem.

264

7837-7843

3313

4694722

The phosphorylation of diphosphoglycerate mutase

1973

Rose, Z.B.; Whalen, R.G.

J. Biol. Chem.

248

1513-1519

3314

4782537

Effects of salt and pH on the rate of erythrocyte diphosphoglycerate mutase

1973

Rose, Z.B.

Arch. Biochem. Biophys.

158

903-910

3318

199431

Purification and properties of 2,3-bisphosphoglycerate phosphatase-mutase from erythrocytes of day-old chicks

1977

Harkness, D.R.; Isaacks, R.E.; Roth, S.C.

Eur. J. Biochem.

78

343-351

3319

163190

Purification of bisphosphoglyceromutase, 2,3-bisphosphoglycerate phosphatase and phosphoglyceromutase from human erthrocytes. Three enzyme activities in one protein

1975

Sasaki, R.; Ikura, K.; Sugimoto, E.; Chiba, H.

Eur. J. Biochem.

50

581-593

3320

166276

2,3-Diphosphoglycerate mutase from human erythrocytes

1975

Rose, Z.B.

Methods Enzymol.

42C

450-454

3323

187124

The purification and kinetic properties of bisphosphoglycerate synthase from horse red blood cells

1976

Rose, Z.B.; Dube, S.

Arch. Biochem. Biophys.

177

284-292

3324

-

Interaction of yeast phosphoglyceromutase with nucleotides

1977

Utsumi, S.; Yano, Y.; Sasaki, R.; Chiba, H.

Agric. Biol. Chem.

41

1852-1862

3326

6297586

Partial characterization of the inactive mutant form of human red cell bisphosphoglyceromutase and comparison with an alkylated form

1983

Rosa, R.; Prehu, M.O.; Albrecht-Ellmer, K.; Calvin, M.C.

Biochim. Biophys. Acta

742

243-249

11537

2165475

Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli

1990

Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R.

J. Bacteriol.

172

4329-4338

11538

9226260

Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803

1997

Valverde, F.; Losada, M.; Serrano, A.

J. Bacteriol.

179

4513-4522

11539

3569291

Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus

1987

Fabry, S.; Hensel, R.

Eur. J. Biochem.

165

147-155

11542

-

Identification of two different glyceraldehyde-3-phosphate dehydrogenases (phosphorylating) in the photosynthetic protist Cyanophora paradoxa

1994

Serrano, A.; Loeffelhardt, W.

Arch. Microbiol.

162

14-19

137612

3899111

Characterization of methylglyoxal synthase in Saccharomyces cerevisiae

1985

Murata, K.; Fukuda, Y.; Watanabe, K.; Saikusa, T.; Shimosaka, M.; Kimura, A.

Biochem. Biophys. Res. Commun.

131

190-198

246772

2834344

Purification and properties of porcine testis acylphosphatase

1987

Fujita, H.; Mizuno, Y.; Shiokawa, H.

J. Biochem.

102

1405-1414

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

246776

3001041

Two isozymes of chicken muscle acylphosphatase: purification and properties

1985

Ohba, Y.; Mizuno, Y.; Takasawa, T.; Shiokawa, H.

J. Biochem.

98

909-919

246781

237200

1,3-Diphosphoglycerate phosphatase

1975

Ramponi, G.

Methods Enzymol.

42C

409-426

246782

238607

Inhibition of horse muscle acylphosphatase by pyridoxal 5'-phosphate

1975

Ramponi, G.; Manao, G.; Camici, G.; White, G.F.

Biochim. Biophys. Acta

391

486-493

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

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

246789

1964788

Purification and characterization of acylphosphatase erythrocyte isoenzyme from turkey muscle

1990

Stefani, M.; Degl'Innocenti, D.; Berti, A.; Cappugi, G.; Manao, G.; Camici, G.; Ramponi, G.

J. Protein Chem.

9

633-640

246790

1647162

Rat muscle acylphosphatase: purification, amino sequence, and immunological characterization

1991

Berti, A.; Tremori, E.; Pazzagli, L.; Degl'Innocenti, D.; Camici, G.; Cappugi, G.; Manao, G.; Ramponi, G.

J. Protein Chem.

10

91-102

246791

8385494

Acylphosphatase induced modifications in the functional properties of erythrocyte membrane sodium pump

1993

Nassi, P.; Marchetti, E.; Nediani, C.; Liguri, G.; Ramponi, G.

Biochim. Biophys. Acta

1147

19-26

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

246793

8276101

Modifications induced by acylphosphatase in the functional properties of heart sarcolemma Na+,K+ pump

1994

Nassi, P.; Nediani, C.; Fiorillo, C.; Marchetti, E.; Liguri, G.; Ramponi,G.

FEBS Lett.

337

109-113

246794

8746632

Expression, purification, and characterization of acylphosphatase muscular isoenzyme as fusion protein with glutathione S-transferase

1995

Modesti, A.; Taddei, N.; Bucciantini, M.; Stefani, M.; Colombini, B.; Raugei, G.; Ramponi, G.

Protein Expr. Purif.

6

799-805

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

246796

8838587

Properties of Cys21-mutated muscle acylphosphatases

1996

Modesti, A.; Taddei, N.; Chiti, F.; Bucciantini, M.; Magherini, F.; Rigacci, S.; Stefani, M.; Raugei, G.; Ramponi, G.

J. Protein Chem.

15

27-34

246797

8886272

Characterization of a novel nucleolytic activity of acylphosphatases

1996

Chiarugi, P.; Raugei, G.; Fiaschi, T.; Taddei, L.; Camici, G.; Ramponi, G.

Biochem. Mol. Biol. Int.

40

73-81

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

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