Ligand 3-phospho-D-glyceroyl phosphate

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Basic Ligand Information

Molecular Structure
Picture of 3-phospho-D-glyceroyl phosphate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C3H8O10P2
3-phospho-D-glyceroyl phosphate
LJQLQCAXBUHEAZ-UWTATZPHSA-N
Synonyms:
1,3-biphosphate-d-glycerate, 1,3-bisphospho-D-glycerate, 1,3-bisphosphoglycerate, 1,3-diphospho-D-glyceric acid, 1,3-diphosphoglycerate, 1,3-diphosphoglyceric acid, 3-phospho-D-glyceroyl 1-phosphate, 3-phospho-D-glyceroyl phosphate., glycerate 1,3-bisphosphate


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

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (14 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
show the reaction diagram
3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
show the reaction diagram
3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate = 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate
-
show the reaction diagram
GDP + 3-phospho-D-glyceroyl 1-phosphate = GTP + 3-phospho-D-glycerate
-
show the reaction diagram
1,3-diphosphoglyceric acid + (polyphosphate)n = 3-phosphoglycerate + (polyphosphate)n+1
-
show the reaction diagram
1,3-diphosphoglycerate + H2O = 3-phosphoglycerate + phosphate
-
show the reaction diagram
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
-

In Vivo Product in Enzyme-catalyzed Reactions (10 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+
-

Substrate in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
3-phospho-D-glyceroyl phosphate + NADPH + H+ = D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
show the reaction diagram
GDP + 3-phospho-D-glyceroyl 1-phosphate = GTP + 3-phospho-D-glycerate
-
show the reaction diagram
1,3-diphosphoglyceric acid + (polyphosphate)n = 3-phosphoglycerate + (polyphosphate)n+1
-
show the reaction diagram
Glucose 1-phosphate + 1,3-bisphosphoglycerate = Glucose 1,6-diphosphate + glycerate 3-phosphate
-

Product in Enzyme-catalyzed Reactions (63 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+
-

Activator in Enzyme-catalyzed Reactions (4 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (7 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
0.385 mM and 0.005 mM, 50% inhibition of PFK I and PFK II respectively, phosphate relieves from inhibition
-

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

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (22 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
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
73.56
-
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
0.14
-
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
0.06
-
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
0.08
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADPH
419
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADH
88
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADPH
223
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADH
40
-
mutant enzyme N336A
23.2
-
wild-type enzyme
mutant enzyme T393A
250
-
mutant enzyme T375A
675
-
mutant enzyme R38A
6
-
mutant enzyme k219A
5.25
-
mutant enzyme K125A
0.78
-
mutant enzyme F165A
1170
-
mutant enzyme E343A
84
-
mutant enzyme E192A
1130
-
25°C
12.5
-
4°C
3.6
-
37°C
23.4
-

KM Value (93 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
0.13
-
enzyme form E9.0, pH 9
0.032
-
enzyme form E9.0, pH 7
0.018
-
enzyme form E8.5, pH 9
0.035
-
enzyme form E8.5, pH 7
0.012
-
enzyme form E6.8, pH 9
0.172
-
enzyme form E6.8, pH 7
0.002
-
enzyme form E6.6, pH 9
0.042
-
enzyme form E6.6, pH 7
0.01
-
cytosolic enzyme
0.14
-
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
0.053
-
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
0.049
-
mutant F36G, pH 8.8, 25°C
0.051
-
mutant F36L, pH 8.8, 25°C
0.049
-
mutant F36T, pH 8.8, 25°C
0.053
-
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
0.051
-
pH 8.0, 36°C, long torpor
pH 8.0, 5°C, euthermic
pH 8.6, temperature not specified in the publication
1.78
-
glyoxysomal enzyme
0.1
-
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
0.036
-
wild-type, pH 8.8, 25°C
0.036
-
mutant enzyme S188A, reaction with NADPH
0.013
-
mutant B(R77A)
0.016
-
mutant B(188)A, analyzed under reducing conditions
0.031
-
with NADPH as coenzyme, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.02
-
mutant enzyme S188A, reaction with NADH
0.012
-
mutant B(E362Q)
0.012
-
mutant enzyme T33A, reaction with NADH
0.012
-
mutant enzyme T33A, reaction with NADPH
0.018
-
mutant enzyme T33A/S188A, reaction with NADH
0.01
-
mutant enzyme T33A/S188A, reaction with NADPH
0.012
-
native enzyme A3-GAPDH, reaction with NADH
0.012
-
native enzyme A3-GAPDH, reaction with NADPH
0.015
-
pH 6.5, 70°C
0.00041
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
5.8
-
with NADH as cofactor, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.016
-
mutant B(188)A, analyzed under oxidizing conditions
0.027
-
AB-GAPDH, analyzed under reducing conditions
0.02
-
AB-GAPDH, analyzed under oxidizing conditions
0.024
-
GapB, analyzed under reducing conditions
0.015
-
B(minCTE) mutant
0.022
-
A(plusCTE) mutant, analyzed under reducing conditions
0.021
-
GapA
0.015
-
GapB, analyzed under oxidizing conditions
0.02
-
A(plusCTE) mutant, analyzed under oxidizing conditions
0.019
-
pH 8.0, 60°C
5.8
-
GapA
0.015
-
AB-GAPDH, analyzed under reducing conditions
0.02
-
AB-GAPDH, analyzed under oxidizing conditions
0.024
-
B(minCTE) mutant
0.022
-
A(plusCTE) mutant, analyzed under reducing conditions
0.021
-
A(plusCTE) mutant, analyzed under oxidizing conditions
0.019
-
GapB, analyzed under oxidizing conditions
0.02
-
mutant B(R77A)
0.016
-
mutant B(E362Q)
0.012
-
GapB, analyzed under reducing conditions
0.015
-
mutant B(188)A, analyzed under reducing conditions
0.031
-
mutant B(188)A, analyzed under oxidizing conditions
0.027
-
25°C, pH 7.5, liver enzyme peak II
0.00028
-
23°C, pH 8, Mg2+-enzyme in brain
0.000087
-
25°C, pH 7.5, liver enzyme peak I
0.00023
-
25°C, pH 7.5, erythrocyte enzyme
0.00045
-
23°C, pH 8, Zn2+-enzyme in brain
0.000091
-
at pH 7.4, temperature not specified in the publication
0.00438
-
mutant enzyme E192A
0.0091
-
mutant enzyme E343A
0.0013
-
wild-type enzyme
mutant enzyme F165A
0.017
-
mutant enzyme K125A
0.0038
-
70°C, pH 6.5
5.6
-
mutant enzyme k219A
0.0077
-
mutant enzyme N336A
0.0022
-
mutant enzyme R38A
0.29
-
at pH 7.4, temperature not specified in the publication
0.00686
-
mutant enzyme T375A
0.003
-
mutant enzyme T393A
0.01
-
at pH 7.0 and 70°C
0.008
-
erythrocyte enzyme
skeletal muscle enzyme
0.62
-
muscle
1.6
-
pH 7.8
0.0007
-
pH 7.5, low salt concentration
0.0005
-
pH 7.2, 0.1 M KCl
0.003
-
pH 7.2
0.0031
-
pH 6.8
0.0036
-

Ki Value (2 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
49.1
-
pH 8.0, 60°C
49.1
-

References & Links

Links to other databases for 3-phospho-D-glyceroyl phosphate

ChEBI
PubChem
-
PubChem