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Ligand 3-phosphoglycerate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

Entner Doudoroff pathway, glycolysis, mannosylglycerate biosynthesis, serine metabolism

KEGG

Biosynthesis of alkaloids derived from histidine and purine, Biosynthesis of alkaloids derived from ornithine, lysine and nicotinic acid, Biosynthesis of alkaloids derived from shikimate pathway, Biosynthesis of alkaloids derived from terpenoid and polyketide, Biosynthesis of amino acids, Biosynthesis of cofactors, Biosynthesis of phenylpropanoids, Biosynthesis of plant hormones, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of terpenoids and steroids, Biosynthesis of various secondary metabolites - part 3, Carbon fixation in photosynthetic organisms, Carbon metabolism, Central carbon metabolism in cancer, Cysteine and methionine metabolism, Glucagon signaling pathway, Glycerolipid metabolism, Glycine, serine and threonine metabolism, Glycolysis / Gluconeogenesis, Glyoxylate and dicarboxylate metabolism, Methane metabolism, Microbial metabolism in diverse environments, Pentose phosphate pathway more

MetaCyc

1-butanol autotrophic biosynthesis (engineered), 3PG-factor 420 biosynthesis, Bifidobacterium shunt, bryostatin biosynthesis, Calvin-Benson-Bassham cycle, D-apionate degradation III (RLP transcarboxylase/hydrolase), Entner-Doudoroff pathway I, Entner-Doudoroff pathway III (semi-phosphorylative), ethene biosynthesis V (engineered), formaldehyde assimilation I (serine pathway), formaldehyde assimilation III (dihydroxyacetone cycle), gluconeogenesis I, gluconeogenesis II (Methanobacterium thermoautotrophicum), gluconeogenesis III, glucosylglycerate biosynthesis I, glycerol degradation to butanol, glycolysis I (from glucose 6-phosphate), glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), glycolysis IV, glycolysis V (Pyrococcus), heterolactic fermentation, L-cysteine biosynthesis IX (Trichomonas vaginalis), L-serine biosynthesis I, L-serine biosynthesis II, mannosylglucosylglycerate biosynthesis I, mannosylglycerate biosynthesis I, nucleoside and nucleotide degradation (archaea), phosalacine biosynthesis, phosphinothricin tripeptide biosynthesis, photorespiration, photosynthetic 3-hydroxybutanoate biosynthesis (engineered), Rapoport-Luebering glycolytic shunt, Rubisco shunt, sucrose biosynthesis I (from photosynthesis), superpathway of glucose and xylose degradation more

Show all BRENDA pathways known for 3-phosphoglycerate

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Roles as Enzyme Ligand

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

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.95

3-phosphoglycerate + NAD+ = 3-phosphohydroxypyruvate + NADH

287551, 287546, 287547, 287548, 287543, 287538, 287545, 287527, 287540, 287549, 656114

-

2.7.2.3

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

761069

-

5.4.2.11

3-Phosphoglycerate = ?

3217, 3231

-

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.9

DL-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-DL-glycerate + NADPH + H+

-

-

2.7.2.3

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

-

-

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

-

-

5.4.2.11

2-Phosphoglycerate = 3-Phosphoglycerate

652877

-

Substrate in Enzyme-catalyzed Reactions (19 results)

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Show Substrate (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.95

3-phosphoglycerate + NAD+ = 3-phosphohydroxypyruvate + NADH

287532, 287526, 287541, 287543, 287544, 287533, 287537, 287530, 287534, 287538, 287545, 287546, 287547, 287548, 287550, 287551, 287380, 287528, 656114, 287529, 287539, 287531, 287527, 287536, 287542, 287540, 287549, 655484, 287525

-

1.1.99.14

glycerate 3-phosphate + 2,6-dichlorophenolindophenol = ?

741190

-

2.7.2.3

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

761069

-

3.1.3.1

3-phosphoglycerate + H2O = glycerol + phosphate

94573, 94595, 94612, 94624, 94596, 94613, 94607

-

3.1.3.10

3-phosphoglycerate + H2O = 2,3-dihydroxypropanoic acid + phosphate

134582, 134580

-

3.1.3.19

3-phosphoglycerate + H2O = glyceric acid + phosphate

94707

-

3.1.3.2

1-glycerate phosphate + H2O = glycerate + phosphate

134766, 134771, 134787, 134736, 134754, 134710

-

3.1.3.2

3-glycerate phosphate + H2O = glycerate + phosphate

134706

-

3.1.3.2

3-phosphoglycerate + H2O = glycerate + phosphate

134771, 665279, 134800, 664662, 665560, 664223, 651143, 706314, 716486

-

3.1.3.2

3-phosphoglycerate + H2O = glycerol + phosphate

682668

-

3.1.3.2

4 entries

3.1.3.20

3-phosphoglycerate + H2O = glycerate + phosphate

81024, 81023

-

3.1.3.25

3-phosphoglycerate + H2O = ?

114220

-

3.1.3.26

3-phosphoglycerate + H2O = glycerate + phosphate

649370, 653826

-

3.1.3.58

3-phosphoglycerate + H2O = glycerate + phosphate

646416

-

3.1.3.60

3-phosphoglycerate + H2O = glycerate + phosphate

134800, 646421

-

3.1.3.8

3-phosphoglycerate + H2O = glycerate + phosphate

649370, 653826, 682302, 677788, 706314

-

5.4.2.11

3-Phosphoglycerate = 2-Phosphoglycerate

3217, 3236, 3246, 3248, 3215, 3231, 3219, 3221, 649656, 651088, 652799, 3229

-

5.4.2.11

3-Phosphoglycerate = ?

3217, 3231

-

5.4.2.11

2 entries

5.4.2.12

3-Phosphoglycerate = 2-Phosphoglycerate

3250, 3241, 3259, 3234

-

Product in Enzyme-catalyzed Reactions (13 results)

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Show Product (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.95

3-phosphohydroxypyruvate + NADH = 3-phosphoglycerate + NAD+

-

-

1.2.1.3

glyceraldehyde 3-phosphate + NAD+ + H2O = glycerate 3-phosphate + NADH

-

-

1.2.1.88

glyceralaldehyde-3-phosphate + NAD+ + H2O = glycerate-3-phosphate + NADH

-

-

1.2.1.9

DL-glyceraldehyde 3-phosphate + NAD+ + H2O = 3-phospho-DL-glycerate + NADH + H+

-

-

1.2.1.9

DL-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-DL-glycerate + NADPH + H+

-

-

1.2.1.9

2 entries

2.7.1.31

ATP + D-glycerate = ADP + 3-phosphoglycerate

-

-

2.7.2.3

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

-

-

2.7.4.17

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

642547

-

3.6.1.7

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

-

-

3.6.1.7

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

-

-

3.6.1.7

2 entries

5.4.2.11

2-Phosphoglycerate = 3-Phosphoglycerate

652877,

-

5.4.2.12

2-Phosphoglycerate = 3-Phosphoglycerate

-

-

5.4.2.2

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

3284

-

Activator in Enzyme-catalyzed Reactions (66 results)

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Show Activating Compound (66 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.27

activation

286441

-

1.2.1.23

slightly activation

288138

-

1.2.7.6

stimulates

644692

-

1.5.3.6

activation of autocatalytical flavinylation

392454

-

2.4.1.18

10 mM, activates

636950

-

2.7.1.1

activates

640249

-

2.7.1.40

allosteric activator. Regulation of the enzyme by a carboxylate molecule rather than a sugar phosphate may reflect a step in the evolution of glycolysis that predates the dominance of sugars in metabolism

727026

-

2.7.1.40

slight activation

641584

-

2.7.1.40

2 entries

2.7.7.10

slight activation

642818

-

2.7.7.27

-

663026, 643164, 643155, 663145, 694714, 706326, 706334, 643167, 643157, 643139, 694731, 704593

-

2.7.7.27

10 mM, 16fold stimulation, enzyme from maize endosperm

663141

-

2.7.7.27

3-PGA

702704, 706322

-

2.7.7.27

50% activation at 0.12 mM for wild-type, at 1.38 mM for mutant D157E, at 0.03 mM for mutant K41R of large subunit plus D143N of small subunit

673678

-

2.7.7.27

50% activation of wild-type at 0.04 mM, of mutation P52L, large subunit, at 0.27 mM, of mutation P52L, large subunit, plus mutation L46F, small subunit at 0.1 mM, of mutation P52L, large subunit, plus mutation P112L, small subunit at 0.14 mM, of mutation P52L, large subunit, plus mutation P308L, small subunit at 0.006 mM, of mutation P52L, large subunit, plus mutation R350K, small subunit at 0.01 mM

671807

-

2.7.7.27

50% of maximal activation for wild-type at 0.11 mM, for mutant P17L at 0.08 mM, for mutant P26L at 0.15 mM, for mutant P44L at 0.25 mM, for mutant P52L at 0.77 mM, for mutant P55L at 0.26 mM, for mutant P66L at 0.03 mM

676387

-

2.7.7.27

A0.5 value for wild-type 0.28 mm, for large subunit E370G/small subunit wild-type 0.83 mM

739280

-

2.7.7.27

activates

663126

-

2.7.7.27

activation

488901, 643144, 643122, 643114, 643141, 643117, 643118, 643119, 643120, 643115, 643116, 643136, 643135, 643137

-

2.7.7.27

activation kinetics. 50% of the maximal velocity at 0.054 mM

721938

-

2.7.7.27

activation kinetics. 50% of the maximal velocity at 0.075 mM

721938

-

2.7.7.27

activation kinetics. Wild-type tetramer, 50% of the maximal velocity at 0.54 mM. Tetramer carrying mutation D148A in small subunit, 50% of the maximal velocity at 0.003 mM. Tetramer carrying mutation D171A in large subunit, 50% of the maximal velocity at 0.067 mM

721938

-

2.7.7.27

activation of leaf enzyme, however endosperm enzyme only, when phosphate, ADP or fructose 1,6-bisphosphate are present

643160

-

2.7.7.27

activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview

694734

-

2.7.7.27

activation of the heterotetramer comprised of large subunit isoform L1 and small subunit S is almost completely dependent on 3-phosphoglycerate. The heterotetramer comprised of large subunit isoform L3 and small subunit S shows approx. 20% of its maximal activity even in the absence of 3-phosphoglycerate

721522

-

2.7.7.27

activation. A0.5 value and Hill coefficient for wild-type 0.076 mM and 1.0, large subunit mutant E38K 0.013 mM and 0.9, large subunit mutant G101N 0.023 mM and 1.0, large subunit mutant E38K/G101N 0.006 mM and 0.4

737860

-

2.7.7.27

activator follows hyberbolic kinetic

643168

-

2.7.7.27

allosteric activation

643122, 643117, 643118, 643119, 643120, 643115, 643116, 643136, 643123

-

2.7.7.27

allosterin activator

693217

-

2.7.7.27

endospermal enzyme

643113

-

2.7.7.27

generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both

676474

-

2.7.7.27

half-maximal activation at 0.25 mM for long day photoperiod, at 0.33 mM at short day photoperiod

723485

-

2.7.7.27

in leaves 2-3fold, DTT decreases the activation

676354

-

2.7.7.27

in leaves 2-3fold, DTT highly decreases the activation

676354

-

2.7.7.27

in leaves 2fold, DTT abolishes the activation at 5 mM

676354

-

2.7.7.27

in leaves 2fold, DTT decreases the activation

676354

-

2.7.7.27

in leaves 30fold, DTT abolishes the activation at 1-5 mM

676354

-

2.7.7.27

in leaves and tubers 1.4-3.8fold, DTT decreases the activation, overview

676354

-

2.7.7.27

in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms. Activation constant Ka is 0.06 for maize enzyme and 0.03 for the chimeric enzyme

737552

-

2.7.7.27

kinetic study and comparison of activation of recombinant enzymes, the activation is more drastic for recombinant enzyme APS1/APL1

643153

-

2.7.7.27

kinetic study at different temperatures

643149

-

2.7.7.27

kinetics

643144, 643123

-

2.7.7.27

minimal activation

643164

-

2.7.7.27

no activation

488901, 643134

-

2.7.7.27

only 2fold stimulation at 15 mM 3-phosphoglycerate

643162

-

2.7.7.27

pH-dependent

643144, 643117

-

2.7.7.27

pH-dependent, endosperm

643144

-

2.7.7.27

presence of 3-phosphoglycerate increases the velocity and the affinity for glucose 1-phosphate for the potato enzymes. Redox state does not affect kcat of the two potato isoforms. Without 3-phosphoglycerate the oxidized potato enzyme exhibits a rapid equilibrium random bi-bi mechanism with a dead end ternary complex. Activation constant Ka is 0.52 for the oxidized and 0.20 for the reduced enzyme and 0.03 for the chimeric enzyme

737552

-

2.7.7.27

recombinant enzyme is insensitive to 3-phosphoglycerate

643165

-

2.7.7.27

slight activation

643135, 643113

-

2.7.7.27

slight activation, DTT abolishes the activation

676354

-

2.7.7.27

strong

643141

-

2.7.7.27

the activities of recombinant maize and recombinant potato enzyme are comparable in the presence of 10 mM 3-phosphoglycerate, however in absence of 3-phosphoglycerate and phosphate the maize enzyme exhibits approximately 20fold more activity than does potato enzyme, in presence of both 3-phosphoglycerate and phosphate the maize enzyme is 47fold active than is the potato enzyme

643157

-

2.7.7.27

the homotetrameric small subunit has much lower affinity for activator than the heterotetrameric enzyme

643147

-

2.7.7.27

the polyethylene glycerol induced molecular crowding increases the sensitivity of enzyme to the cross-talk between 3-phosphoglycerate and phosphate, the ultrasensitive behaviour is correlated with intramolecular conformational changes induced in the tertiary structure of the homotetrameric enzyme

643159

-

2.7.7.27

very little enzymatic activity in the absence of 3-phosphoglycerate, 40fold in catalytic activity, when assayed und near saturating 3-phosphoglycerate concentration

643156

-

2.7.7.27

wild-type, half-maximal activation at 0.016 mM, mutant A33K, at 0.0055 mM, mutant G96N, at 0.0064 mM, mutant A33K/G96N, at 0.0066 mM

676664

-

2.7.7.27

-

706407

-

2.7.7.27

48 entries

2.7.7.9

slight activation

642818

-

3.1.3.46

-

94937

-

3.1.3.63

-

646445

-

3.1.3.63

activation

646440

-

3.1.3.63

2 entries

3.2.1.1

50 mM, 5fold activation of muscle alpha-amylase

654030

-

4.1.1.31

slight stimulation

656978

-

4.1.1.31

-

4307

-

4.1.1.31

activates

4301

-

4.1.1.31

3 entries

5.4.2.4

required, can be substituted by 2-phosphoglycerate

3323

-

Inhibitor in Enzyme-catalyzed Reactions (57 results)

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Show Inhibitors (57 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.27

-

286447

-

1.1.1.399

noncompetitive inhibition

287546

-

1.1.1.42

-

286796

-

1.1.1.44

about 40% residual activity at 5 mM

741367

-

1.1.1.95

-

287546

-

1.1.1.95

noncompetitive to phosphohydroxypyruvate

287540

-

1.1.1.95

2 entries

1.4.7.1

-

392005

-

1.5.1.17

-

13374

-

2.2.1.6

noncompetitive

395918

-

2.7.1.1

-

640251

-

2.7.1.1

feedback regulation

758866, 758986

-

2.7.1.1

hexokinase III

640241

-

2.7.1.1

3 entries

2.7.1.105

-

640345

-

2.7.1.106

-

640350

-

2.7.1.106

weak

640348

-

2.7.1.11

-

640422, 640443

-

2.7.1.11

0.9 mM, 50% inhibition of plastid PFK

640440

-

2.7.1.11

1 mM, complete inhibition, phosphate relieves, 0.5 mM, 50% inhibition, sigmoidal inhibition curve; inhibition kinetics

640447

-

2.7.1.11

1.5-2.0 mM, 50% inhibition

640521

-

2.7.1.11

2 mM, 86% inhibition; inhibition kinetics

640448

-

2.7.1.11

about 70% inhibition at 7 mM

704345

-

2.7.1.11

mixed inhibition

672415

-

2.7.1.106

2 entries

2.7.1.11

7 entries

2.7.1.165

-

641338

-

2.7.1.19

74% inhibition at 6 mM and pH 7.2

641020

-

2.7.1.31

-

641341, 641343

-

2.7.1.40

-

641576

-

2.7.1.40

8% inhibition at 5 mM

723044

-

2.7.1.40

80% activity at pH 6.4, 86% activity at pH 7.4

676689

-

2.7.1.40

not

641565

-

2.7.1.40

4 entries

2.7.1.90

-

642086

-

2.7.11.5

-

640609

-

2.7.3.9

-

642510

-

2.7.7.27

inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations

676561

-

2.7.7.42

66% inhibition at 20 mM

643331

-

2.7.7.59

inhibits uridylyl removing activity

643541

-

2.7.7.9

no inhibition of UDP-glucose synthesis

643742

-

3.1.3.25

weak competetive inhibitor

114219

-

3.1.3.60

-

646427

-

3.1.3.60

competitive

646423

-

3.1.3.60

competitive; complete inhibition at 5 mM

646421

-

3.1.3.60

3 entries

3.6.1.21

-

657184

-

3.6.1.7

-

246781

-

3.6.1.7

erythrocyte isoenzyme, competitive inhibition, Ki: 1.70 mM

246792

-

3.6.1.7

heart enzyme, 5 mM: 8% inhibition, substrate: 1,3-diphosphoglycerate

246781

-

3.6.1.7

3 entries

4.1.1.31

-

4318

-

4.1.1.49

-

649304

-

4.1.1.5

alpha-acetolactate synthetase and alpha-acetolactate decarboxylase are measured together

4647

-

4.1.2.13

-

4943

-

4.1.3.1

-

33118

-

4.1.3.1

29% inhibition at 1 mM

33121

-

4.1.3.1

2 entries

4.2.3.3

-

137600, 137601, 137602, 137603, 137612

-

5.3.1.1

-

2565

-

5.3.1.1

binding at the active site with the dimer-interface site showing strong electrostatic anchoring of the phosphate group involving the Arg98 and Lys112 residues of TIM, comparisons of binding structures at the interface, overview

701474

-

5.3.1.1

2 entries

5.3.1.6

-

2792

-

5.3.1.9

-

2867

-

5.4.2.2

uncompetitive inhibition

650261

-

5.4.2.4

-

3318

-

3D Structure of Enzyme-Ligand-Complex (PDB) (78 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (78 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.37

6cwa, 3D-view

1.1.1.399

6cwa, 3D-view

1.1.1.44

4gwk, 3D-view

1.1.1.95

4njm, 3D-view

1.1.1.95

6cwa, 3D-view

1.2.1.12

3ksz, 3D-view

1.2.1.12

3kv3, 3D-view

1.2.1.12

3l4s, 3D-view

2.4.1.266

4y6n, 3D-view

2.4.1.266

4y6u, 3D-view

2.4.1.266

4y9x, 3D-view

2.4.1.266

5jqx, 3D-view

2.7.2.3

13pk, 3D-view

2.7.2.3

1hdi, 3D-view

2.7.2.3

1kf0, 3D-view

2.7.2.3

1qpg, 3D-view

2.7.2.3

1vpe, 3D-view

2.7.2.3

2cun, 3D-view

2.7.2.3

2p9t, 3D-view

2.7.2.3

2paa, 3D-view

2.7.2.3

2wzb, 3D-view

2.7.2.3

2wzc, 3D-view

2.7.2.3

2wzd, 3D-view

2.7.2.3

2x13, 3D-view

2.7.2.3

2x14, 3D-view

2.7.2.3

2x15, 3D-view

2.7.2.3

2xe6, 3D-view

2.7.2.3

2xe7, 3D-view

2.7.2.3

2xe8, 3D-view

2.7.2.3

2y3i, 3D-view

2.7.2.3

2ybe, 3D-view

2.7.2.3

3c39, 3D-view

2.7.2.3

3c3a, 3D-view

2.7.2.3

3c3c, 3D-view

2.7.2.3

3pgk, 3D-view

2.7.2.3

3zoz, 3D-view

2.7.2.3

4axx, 3D-view

2.7.2.3

4o33, 3D-view

2.7.2.3

4o3f, 3D-view

2.7.2.3

5m3u, 3D-view

2.7.2.3

5m6z, 3D-view

2.7.2.3

5mxm, 3D-view

2.7.2.3

5np8, 3D-view

2.7.2.3

6hxe, 3D-view

1.1.1.95

2 entries

1.2.1.12

3 entries

2.4.1.266

4 entries

2.7.2.3

32 entries

2.7.5.3

3pgm, 3D-view

3.1.3.13

2f90, 3D-view

3.1.3.13

2h4x, 3D-view

3.1.3.13

2h52, 3D-view

3.1.3.13

2hhj, 3D-view

3.1.3.13

4 entries

3.5.1.87

5i4m, 3D-view

4.1.1.39

1aa1, 3D-view

4.1.1.39

1rus, 3D-view

4.1.1.39

2 entries

4.1.2.14

5xsf, 3D-view

5.3.1.1

1iih, 3D-view

5.3.1.1

1m7o, 3D-view

5.3.1.1

2vfe, 3D-view

5.3.1.1

2vfg, 3D-view

5.3.1.1

2vfh, 3D-view

5.3.1.1

2vfi, 3D-view

5.3.1.1

2x2g, 3D-view

5.3.1.1

3uww, 3D-view

5.4.2.1

1ejj, 3D-view

5.4.2.1

1qhf, 3D-view

5.4.2.1

2f90, 3D-view

5.4.2.1

2h4x, 3D-view

5.4.2.1

2h52, 3D-view

5.4.2.1

2hhj, 3D-view

5.4.2.1

3fdz, 3D-view

5.4.2.1

3gp5, 3D-view

5.4.2.1

3igy, 3D-view

5.4.2.1

3igz, 3D-view

5.4.2.12

4nwj, 3D-view

5.4.2.12

5vpu, 3D-view

5.4.2.4

2a9j, 3D-view

5.4.2.4

2f90, 3D-view

5.4.2.4

2h4x, 3D-view

5.4.2.4

2h52, 3D-view

5.4.2.4

2hhj, 3D-view

5.3.1.1

8 entries

5.4.2.1

10 entries

5.4.2.12

2 entries

5.4.2.4

5 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (16 results)

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Show Turnover Number (16 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.7.2.3

1.29

-

mutant enzyme H111A, at pH 7.5 and 25°C

761069

2.7.2.3

1.3

-

mutant enzyme H71A, at pH 7.5 and 25°C

761069

2.7.2.3

1.35

-

mutant enzyme H89A, at pH 7.5 and 25°C

761069

2.7.2.3

1.37

-

wild type enzyme, at pH 7.5 and 25°C

761069

2.7.2.3

3.2

-

mutant enzyme H71A, at pH 5.5 and 25°C

761069

2.7.2.3

3.2

-

mutant enzyme H89A, at pH 5.5 and 25°C

761069

2.7.2.3

3.6

-

mutant enzyme H57A, at pH 5.5 and 25°C

761069

2.7.2.3

3.7

-

wild type enzyme, at pH 5.5 and 25°C

761069

2.7.2.3

3.8

-

mutant enzyme H111A, at pH 5.5 and 25°C

761069

2.7.2.3

4.4

-

mutant enzyme H57A, at pH 7.5 and 25°C

761069

5.4.2.11

0.078

-

mutant H181A

3230

5.4.2.11

2.1

-

mutant S11G

3231

5.4.2.11

324

-

mutant K246G

3231

5.4.2.11

384

-

wild-type enzyme

3231

5.4.2.11

490

-

wild-type enzyme

3230

5.4.2.11

530

-

-

652799

2.7.2.3

10 entries

5.4.2.11

6 entries

K_M Value (35 results)

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Show KM Value (35 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.95

0.212

-

pH 9.0

655484

2.7.2.3

0.48

-

mutant enzyme H111A, at pH 7.5 and 25°C

761069

2.7.2.3

0.49

-

mutant enzyme H71A, at pH 7.5 and 25°C

761069

2.7.2.3

0.511

-

mutant enzyme H57A, at pH 7.5 and 25°C

761069

2.7.2.3

0.517

-

mutant enzyme H89A, at pH 7.5 and 25°C

761069

2.7.2.3

0.53

-

wild type enzyme, at pH 7.5 and 25°C

761069

2.7.2.3

0.61

-

mutant enzyme H57A, at pH 5.5 and 25°C

761069

2.7.2.3

0.63

-

mutant enzyme H89A, at pH 5.5 and 25°C

761069

2.7.2.3

0.638

-

mutant enzyme H111A, at pH 5.5 and 25°C

761069

2.7.2.3

0.661

-

wild type enzyme, at pH 5.5 and 25°C

761069

2.7.2.3

0.68

-

mutant enzyme H71A, at pH 5.5 and 25°C

761069

3.1.3.2

0.08

-

-

134800

3.1.3.2

0.27

-

-

134771

3.1.3.2

6

-

pH 5.3, 25°C, SAP2

651143

2.7.2.3

10 entries

3.1.3.2

3 entries

3.1.3.60

1.21

-

25°C, pH 5.6

646421

5.4.2.11

0.026

-

H181A mutant

3230

5.4.2.11

0.1

-

MB-type and BB-type isozymes

3248

5.4.2.11

0.2

-

MM-type isozyme

3248

5.4.2.11

0.22

-

-

3251

5.4.2.11

0.56

-

-

652799

5.4.2.11

0.58

-

-

651088, 652799

5.4.2.11

0.58

-

mutase activity

649656

5.4.2.11

0.65

-

wild-type enzyme

3231

5.4.2.11

0.67

-

mutant S11G

3231

5.4.2.11

0.68

-

mutant K246G

3231

5.4.2.11

0.74

-

wild-type enzyme

3230

5.4.2.11

1.25

-

E93D mutant

651088

5.4.2.11

1.3

-

-

3229

5.4.2.11

1.54

-

R14Q mutant

651088

5.4.2.11

2.64

-

R120Q mutant

651088

5.4.2.11

4.9

-

R121Q mutant

651088

5.4.2.11

5.26

-

R120Q/R121Q double mutant

651088

5.4.2.11

7.46

-

R94Q mutant

651088

5.4.2.12

0.324

-

-

3234

5.4.2.12

1.1

-

-

3250, 3241

5.4.2.11

18 entries

5.4.2.12

2 entries

K_i Value (15 results)

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Show KI Value (15 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.399

12.7

-

at pH 7.5 and 37°C

287546

2.7.1.1

12

-

hexokinase III, at 30°C, pH 7.2

640241

2.7.1.1

21

-

at 30°C, pH 8.1

640251

2.7.1.1

2 entries

2.7.1.105

0.084

-

pH 7.8, 25°C

640345

2.7.1.11

0.0207

-

Ki(slope)

672415

2.7.1.11

0.0679

-

Ki(intercept)

672415

2.7.1.11

2.1

-

pH 7.9

640422

2.7.1.11

3 entries

2.7.1.90

0.25

-

pH 7.5

642086

2.7.11.5

1

-

pH 7.5, 37°C, wild-type, kinase activity

640609

2.7.11.5

4

-

pH 7.5, 37°C, mutant AceK4, kinase activity

640609

2.7.11.5

20

-

pH 7.5, 37°C, mutant AceK3, kinase activity

640609

3.1.3.60

0.05

-

25°C, pH 5.6

646421

3.1.3.60

3.3

-

competitive, 30°C, pH 8.5

646423

5.3.1.1

1.9

-

pH 7.6, wild-type enzyme

701474

5.3.1.1

5

-

above, pH 7.6, mutants F96W, F96S, and F96H

701474

2.7.11.5

3 entries

3.1.3.60

2 entries

5.3.1.1

2 entries

References & Links

Literature References (220)

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Show Reference (220 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2565

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Pea seed triose phosphate isomerase

1979

Tomlinson, J.D.; Turner, J.F.

Phytochemistry

18

1959-1962

2792

16668459

Purification and characterization of pea chloroplastic phosphoriboseisomerase

1991

Skrukrud, C.L.; Gordon, I.M.; Dorwin, S.; Yuan, X.H.; Johansson, G.; Anderson, L.E.

Plant Physiol.

97

730-735

2867

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Competitive inhibition of spinach leaf phosphoglucose isomerase isoenzymes by erythrose 4-phosphate

1997

Backhausen, J.E.; Jöstingmeyer, P.; Scheibe, R.

Plant Sci.

130

121-131

3215

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Phosphoglyceric acid mutases

1962

Grisolia, S.

Methods Enzymol.

5

236-242

3217

9365161

Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumors

1997

Durany, N.; Joseph, J.; Cruz-Sanchez, F.F.; Carreras, J.

Br. J. Cancer

76

1139-1149

3219

8736982

The reaction of phosphoglycerate mutase from Schizosaccharomyces pombe with diethylpyrocarbonate

1996

Price, R.M.; Nairn, J.; Price, N.C.; Fothergill-Gilmore, L.A.

Biochem. Soc. Trans.

24

324S

3221

8765231

Phosphoglycerate mutase from Schizosaccharomyces pombe: development of an expression system and characterisation of three histidine mutants of the enzyme

1996

Nairn, J.; Price, N.C.; Kelly, S.M.; Rigden, D.; Fothergill-Gilmore, L.A.; Krell, T.

Biochim. Biophys. Acta

1296

69-75

3229

1530847

Phosphoglycerate mutase from Streptomyces coelicolor A3(2): purification and characterization of the enzyme and cloning and sequence analysis of the gene

1992

White, P.J.; Nairn, J.; Price, N.C.; Nimmo, H.G.; Coggins, J.R.; Hunter, I.S.

J. Bacteriol.

174

434-440

3230

1386023

Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase

1992

White, M.F.; Fothergill-Gilmore, L.A.

Eur. J. Biochem.

207

709-714

3231

2165932

Mutase versus synthase: the phosphoglycerate mutase family studied by protein engineering

1990

White, M.; Fothergill-Gilmore L.A.

Biochem. Soc. Trans.

18

257

3234

2480892

Purification, characterization and immunological properties of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize (Zea mays) seeds

1989

Grana, X.; Urena, J.; Ludevid, D.; Carreras, J.; Climent, F.

Eur. J. Biochem.

186

149-153

3236

2844269

Immunological properties of rat phosphoglycerate mutase isozymes

1988

Castella, J.; Urena, J.; Ludevid, D.; Carreras, J.; Climent, F.

Biochim. Biophys. Acta

956

97-102

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

3248

6293580

Purification and characterization of phosphoglycerate mutase isozymes from pig heart

1982

Bartrons, R.; Carreras, J.

Biochim. Biophys. Acta

708

167-177

3250

33963

Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis

1979

Watabe, K.; Freese, E.

J. Bacteriol.

137

773-778

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

3259

-

Phosphoglycerate mutase from wheat germ (2,3-PGA-independent)

1975

Grisolia, S.; Carreras, J.

Methods Enzymol.

42

429-435

3284

-

Multifunctional properties of beef liver phosphoglucomutase

1976

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

Agric. Biol. Chem.

40

2433-2439

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

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

4301

16664628

Purification and properties of phosphoenolpyruvate carboxylase from immature pods of chickpea (Cicer arietinum L.)

1986

Singal, H.R.; Singh, R.

Plant Physiol.

80

369-373

4307

3093461

Purification and characterization of phosphoenolpyruvate carboxylase from a cyanobacterium

1986

Owttrim, G.W.; Colman, B.

J. Bacteriol.

168

207-212

4318

16667849

Metabolite regulation of partially purified soybean nodule phosphoenolpyruvate carboxylase

1990

Schuller, K.A.; Turpin, D.H.; Plaxton, W.C.

Plant Physiol.

94

1429-1435

4647

16345676

Effects of pH and sugar on acetoin production from citrate by Leuconostoc lactis

1981

Cogan, T.M.; O'Dowd, M.; Mellerick, D.

Appl. Environ. Microbiol.

41

1-8

4943

7872790

Properties of fructose-1,6-bisphosphate aldolase from Escherichia coli: an NMR analysis

1995

Szwergold, B.S.; Ugurbil, K.; Brown, T.R.

Arch. Biochem. Biophys.

317

244-252

13374

-

Alanopine dehydrogenase: purification and characterization of the enzyme from Littorina littorea foot muscle

1982

Plaxton, W.C.; Storey, K.B.

J. Comp. Physiol.

149

57-65

33118

3281659

Purification and regulatory properties of isocitrate lyase from Escherichia coli ML308

1988

Mackintosh, C.; Nimmo, H.G.

Biochem. J.

250

25-31

33121

-

Purification and some properties of isocitrate lyase from the pollen of Pinus densiflora Sieb. et Zucc.

1986

Tsukamoto, C.; Ejiri, S.I.; Katsumata, T.

Agric. Biol. Chem.

50

409-416

81023

6271379

2-Phosphoglycerate phosphatase and serine biosynthesis in Veillonella alcalescens

1981

Pestka, J.J.; Delwiche, E.A.

Can. J. Microbiol.

27

808-814

81024

4284998

2-Phosphoglyceric acid phosphatase: identification and properties of the beef-liver enzyme

1965

Fallon, H.J.; Byrne, W.L.

Biochim. Biophys. Acta

105

43-53

94573

-

Mammalian alkaline phosphatases

1971

Fernley, H.N.

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

4

417-447

94595

3794650

Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor

1986

Hulett, F.M.; Stuckmann, K.; Spencer, D.B.; Sanopoulou, T.

J. Gen. Microbiol.

132

2387-2395

94596

-

Purification and characterization of the outer membrane associated alkaline phosphatase of Lysobacter enzymogenes

1986

von Tigerstrom R.G.; Stelmaschuk, S.

J. Gen. Microbiol.

132

1379-1387

94607

-

Multiple forms and some properties of alkaline phosphatase produced by Aspergillus oryzae on solid medium

1981

Sakurai, Y.; Toda, K.; Shiota, H.

Agric. Biol. Chem.

45

1959-1967

94612

718947

Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization

1978

Schaffel, S.D.; Hulett, F.M.

Biochim. Biophys. Acta

526

457-467

94613

413579

Properties of alkaline phosphatase of the halotolerant yeast Debaryomyces hansenii

1978

Adler, L.

Biochim. Biophys. Acta

522

113-121

94624

2117573

Purification and characterization of alkaline phosphatase of Bacteroides gingivalis 381

1990

Yamashita, Y.; Toyoshima, K.; Yamazaki, M.; Hanada, N.; Takehara, T.

Infect. Immun.

58

2882-2887

94707

-

2-Phosphoglycerol phosphatase

1966

Rao, N.A.; Vaidynathan, C.S.

Methods Enzymol.

9

642-6446

94937

-

6-Phosphofructo-2-kinase and D-fructose-2,6-bisphosphatase activities in mung bean seedlings

1984

Avigad, G.; Bohrer, P.J.

Biochim. Biophys. Acta

798

317-324

114219

16662572

Myo-inositol-1-phosphatase from the pollen of Lilium longiflorum Thunb.

1982

Loewus, M.W.; Loewus, F.A.

Plant Physiol.

70

765-770

114220

6272635

Studies on avian erythrocyte metabolism: purification and properties of myo-inositol 1-phosphatase from chick erythrocytes

1981

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

Arch. Biochem. Biophys.

210

465-473

134580

13839934

The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds

1960

Turner, D.H.; Turner, J.F.

Biochem. J.

74

486-491

134582

13249953

A hexose-1-phosphatase in silkworm blood

1955

Faulkner, P.

Biochem. J.

60

590-596

134706

16665451

Purification and properties of acid phosphatase-1 from a nematode resistant tomato cultivar

1987

Paul, E.M.; Williamson, V.M.

Plant Physiol.

84

399-403

134710

-

Purification and molecular properties of an acid phosphatase from Asclepias curassavica latex

1986

Giordani, R.; Nari, J.; Noat, G.; Sauve, P.

Plant Sci.

43

207-212

134736

7283439

Isolation and properties of an acid phosphatase from thylakoid membranes of Sorghum vulgare

1981

Rengasamy, A.; Selvam, R.; Gnanam, A.

Arch. Biochem. Biophys.

209

230-236

134754

-

Acid phosphatase isoenzymes of Xenopus laevis tadpole tails. Separation and partial characterization

1973

Filburn, C.R.

Arch. Biochem. Biophys.

159

683-693

134766

4235424

Properties of an acid phosphatase in Escherichia coli

1968

Hafkenscheid, J.C.M.

Biochim. Biophys. Acta

167

582-589

134771

14408027

Purification and properties of a nonspecific acid phosphatase from wheat germ

1960

Joyce, B.K.; Grisolia, S.

J. Biol. Chem.

235

2278-2280

134787

9300805

Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds

1997

Olczak, M.; Watorek, W.; Morawiecka, B.

Biochim. Biophys. Acta

1341

14-25

134800

1897950

Purification, characterization, and subcellular localization of an acid phosphatase from black mustard cell-suspension cultures: comparison with phosphoenolpyruvate phosphatase

1991

Duff, S.M.G.; Lefebvre, D.D.; Plaxton, W.C.

Arch. Biochem. Biophys.

286

226-232

137600

11945670

The regulation of Escherichia coli methylglyoxal synthase a new control site in glycolysis

1971

Hopper, D.J.; Cooper, R.A.

FEBS Lett.

13

213-216

137601

4563643

The purification and properties of Escherichia coli methylglyoxal synthase

1972

Hopper, D.J.; Cooper, R.A.

Biochem. J.

128

321-329

137602

4368914

Methylglyoxal formation during glucose catabolism by Pseudomonas saccharophila. Identification of methylglyoxal synthase

1974

Cooper, R.A.

Eur. J. Biochem.

44

81-86

137603

236480

Methylglyoxal synthase

1975

Cooper, R.A.

Methods Enzymol.

41B

502-508

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

246781

237200

1,3-Diphosphoglycerate phosphatase

1975

Ramponi, G.

Methods Enzymol.

42C

409-426

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

286441

4144124

Purification and properties of L(+)-lactate dehydrogenase from potato tubers

1972

Davies, D.D.; Davies, S.

Biochem. J.

129

831-839

286447

7316976

L-Lactate dehydrogenase from leaves of higher plants. Kinetics and regulation of the enzyme from lettuce (Lactuca sativa L)

1981

Betsche, T.

Biochem. J.

195

615-622

286796

3337829

Purification and characterization of NADP+-linked isocitrate dehydrogenase from an alkalophilic Bacillus

1988

Shikata, S.; Ozaki, K.; Kawai, S.; Ito, S.; Okamoto, K.

Biochim. Biophys. Acta

952

282-289

287380

11946015

Glycine and serine inhibition of D-glycerate dehydrogenase and 3-phosphoglycerate dehydrogenase of rat brain

1971

Uhr, M.L.; Sneddon, M.K.

FEBS Lett.

17

137-140

287525

4384871

The mechanism of end product inhibition of serine biosynthesis. I. purification and kinetics of phosphoglycerate dehydrogenase

1968

Sugimoto, E.; Pizer, L.I.

J. Biol. Chem.

243

2081-2089

287526

-

The occurence of D-3-phosphoglycerate dehydrogenase in animal tissues

1964

Willis, J.E.; Sallach, H.J.

Biochim. Biophys. Acta

81

39-54

287527

236449

3-Phosphoglycerate dehydrogenase from seedlings of Pisum sativum

1975

Slaughter, J.C.; Davies, D.D.

Methods Enzymol.

41

278-281

287528

165384

D-3-Phosphoglycerate dehydrogenase from hog spinal cord-1

1975

Feld, R.D.; Sallach, H.J.

Methods Enzymol.

41

282-285

287529

165385

D-3-Phosphoglycerate dehydrogenase from wheat germ-1

1975

Rosenblum, I.Y.; Sallach, H.J.

Methods Enzymol.

41

285-289

287530

-

3-Phosphoglycerate dehydrogenase (Escherichia coli)

1971

Pizer, L.I.; Sugimoto, E.

Methods Enzymol.

17B

325-331

287531

6077050

The serine biosynthetic pathway in Neurospora crassa

1967

Sojka, G.A.; Garner, H.R.

Biochim. Biophys. Acta

148

42-47

287532

13923751

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