1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
This is an abbreviated version!
For detailed information about glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), go to the full flat file.
Word Map on EC 1.2.1.12
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1.2.1.12
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tetramer
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chloroplast
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gapcs
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streptococcal
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stearothermophilus
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glomerulonephritis
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nadp-dependent
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genorm
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normfinder
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medicine
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3-phosphoglycerate
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phosphofructokinase
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flagellum
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poststreptococcal
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1,3-bisphosphoglycerate
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bestkeeper
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lobster
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glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
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4.1.2.13
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plr
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2.7.2.3
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endocapillary
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drug development
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agriculture
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biofuel production
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analysis
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synthesis
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biotechnology
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pharmacology
- 1.2.1.12
- tetramer
- chloroplast
-
gapcs
- streptococcal
- stearothermophilus
- glomerulonephritis
-
nadp-dependent
-
genorm
-
normfinder
- medicine
- 3-phosphoglycerate
-
phosphofructokinase
- flagellum
-
poststreptococcal
- 1,3-bisphosphoglycerate
-
bestkeeper
- lobster
- glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
-
4.1.2.13
- plr
-
2.7.2.3
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endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
Reaction
Synonyms
3-phosphoglyceraldehyde dehydrogenase, A4-GAPDH, A4-glyceraldehyde-3-phosphate dehydrogenase, AB-GAPDH, AnBn-GAPDH, AsGAPDH, At3g04120, BARS-38, CbbG, CgGAP, Clo1313_2095, complement-C3-binding protein, CP 17/CP 18, Ctherm_Gapdh, cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase, cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), dehydrogenase, glyceraldehyde phosphate, dihydrogenase, glyceraldehyde phosphate, EcGAPDH, EcGAPDH1, FgGAPDH, FhGAPDH, G3PD, G3PDH, Ga3P dehydrogenase, Ga3PDHase, GADPH, GAP, GAP1, gap2, GapA, GapB, GAPC, GapC-1, GapC1, GapC2, GAPCp, GAPCp1, GAPCp2, GAPD, GAPDH, GAPDH type 1, GAPDH1, GAPDH2, GAPDH3, GAPDHS, GAPDS, GAPN, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase-S, glyceraldehyde phosphate dehydrogenase (NAD), glyceraldehyde-3 phosphate dehydrogenase, glyceraldehyde-3-P-dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NAD), glyceraldehyde-3-phosphate dehydrogenase 1, glyceraldehyde-3-phosphate dehydrogenase, type I, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS, glyceraldehyde-3-phosphate dehydrogenases, GPD, GPD2, Gra3PDH, GraP-DH, H.c-C3BP, hGAPDH, HsGAPDH, kmGAPDH1p, Larval antigen OVB95, Major larval surface antigen, Mtb-GAPDH, NAD+-dependent GAPDH, NAD+-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-G-3-P dehydrogenase, NAD+-GAPDH, NAD-dependent Ga3PDHase, NAD-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent glyceraldehyde phosphate dehydrogenase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-G3PDH, NAD-GAPDH, NADH-glyceraldehyde phosphate dehydrogenase, P-37, p-GAPDH, PfGAPDH, phosphoglyceraldehyde dehydrogenase, phosphorylating NAD+-dependent GAPDH, Plasmin receptor, Plasminogen-binding protein, plastidial glyceraldehyde-3-phosphate dehydrogenase, pmGAPDH, PyGapdh, rmGAPDH, Rv1436, somatic GAPD, somatic glyceraldehyde 3-phosphate dehydrogenase, sperm-specific GAPDS, sperm-specific glyceraldehyde 3-phosphate dehydrogenase, sperm-specific glyceraldehyde-3-phosphate dehydrogenase, TaeNAD-GAPDH, TagapC, TDH1, TDH2, TDH3, TLAb, triose phosphate dehydrogenase, UDG, uracil-DNA glycosylase, vGPD
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1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)Advanced search results
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results (KM Value
KM Value on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.31
acetaldehyde
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C
0.036
3-phospho-D-glyceroyl phosphate
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
3-phospho-D-glyceroyl phosphate
wild-type, pH 8.8, 25°C
0.049
3-phospho-D-glyceroyl phosphate
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
3-phospho-D-glyceroyl phosphate
mutant F36L, pH 8.8, 25°C
0.051
3-phospho-D-glyceroyl phosphate
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
3-phospho-D-glyceroyl phosphate
mutant F36G, pH 8.8, 25°C
0.053
3-phospho-D-glyceroyl phosphate
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
3-phospho-D-glyceroyl phosphate
mutant F36T, pH 8.8, 25°C
1.78
3-phospho-D-glyceroyl phosphate
Q81X74, YP_027084
pH 8.6, temperature not specified in the publication
0.00046
D-glyceraldehyde 3-phosphate
N-terminally truncated mutant, pH 8.5, 25°C
0.0102
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C
0.0108
D-glyceraldehyde 3-phosphate
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in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C
0.0393
D-glyceraldehyde 3-phosphate
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in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C
0.064
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant wild-type enzyme
0.074
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S66A
0.08
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S205D
0.097
D-glyceraldehyde 3-phosphate
recombinant dN-GAPDS enzyme, pH 8.9, 20°C
0.098
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S205A
0.111
D-glyceraldehyde 3-phosphate
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.111
D-glyceraldehyde 3-phosphate
wild-type, pH 8.8, 25°C
0.147
D-glyceraldehyde 3-phosphate
-
in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C
0.149
D-glyceraldehyde 3-phosphate
-
pH 7.3, enzyme isolated of healthy patients
0.149
D-glyceraldehyde 3-phosphate
mutant enzyme F37L, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.149
D-glyceraldehyde 3-phosphate
mutant F36L, pH 8.8, 25°C
0.153
D-glyceraldehyde 3-phosphate
pH and temperature not specified in the publication
0.156
D-glyceraldehyde 3-phosphate
mutant enzyme F37G, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.156
D-glyceraldehyde 3-phosphate
mutant F36G, pH 8.8, 25°C
0.159
D-glyceraldehyde 3-phosphate
-
pH 8.0, enzyme isolated of healthy patients
0.161
D-glyceraldehyde 3-phosphate
mutant enzyme F37T, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.161
D-glyceraldehyde 3-phosphate
mutant F36T, pH 8.8, 25°C
0.188
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S124A
0.21
D-glyceraldehyde 3-phosphate
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in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.24
D-glyceraldehyde 3-phosphate
recombinant dN-GAPDS enzyme mutant D311N, pH 8.9, 20°C
0.25
D-glyceraldehyde 3-phosphate
recombinant enzyme, pH and temperature not specified in the publication
0.25
D-glyceraldehyde 3-phosphate
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.27
D-glyceraldehyde 3-phosphate
recombinant wild-type enzyme, pH 8.9, 20°C
0.31
D-glyceraldehyde 3-phosphate
wild type enzyme, pH 8.7, 25°C
0.32
D-glyceraldehyde 3-phosphate
mutant enzyme H178N, pH 8.7, 25°C
0.34
D-glyceraldehyde 3-phosphate
mutant enzyme C151S, pH 8.7, 25°C
0.34
D-glyceraldehyde 3-phosphate
mutant enzyme C151S/H178N, pH 8.7, 25°C
0.46
D-glyceraldehyde 3-phosphate
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.5
D-glyceraldehyde 3-phosphate
immobilized enzyme reactor, at pH 7.5 and 25°C
0.5
D-glyceraldehyde 3-phosphate
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.763
D-glyceraldehyde 3-phosphate
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication
0.77
D-glyceraldehyde 3-phosphate
in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0
1
D-glyceraldehyde 3-phosphate
mutant enzyme D186G and mutant enzyme S48G
1.44
D-glyceraldehyde 3-phosphate
pH 7.4, 37°C, recombinant enzyme
1.45
D-glyceraldehyde 3-phosphate
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C
1.78
D-glyceraldehyde 3-phosphate
Q81X74, YP_027084
at pH 8.5, temperature not specified in the publication
3.7
D-glyceraldehyde 3-phosphate
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immobilized enzyme reactor, at pH 8.6 and 25°C
3.7
D-glyceraldehyde 3-phosphate
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enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.0734
D-Glyceraldehyde-3-phosphate
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in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.5
D-Glyceraldehyde-3-phosphate
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GAPDH immobilized on an octyl silica column
0.000032
NAD+
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication
0.022
NAD+
in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0
0.025
NAD+
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in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.057
NAD+
-
recombinant enzyme, in the presence of D-glyceraldehyde 3-phosphate, in 50 mM Tricine buffer (pH 8.5), at 25°C
0.058
NAD+
pH 8.0, 25°C, recombinant mutant D35G/L36T/P192S
0.059
NAD+
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.06
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant Y283V
0.064
NAD+
-
in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C
0.088
NAD+
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of glyceraldehyde, at 25°C
0.092
NAD+
-
in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.1
NAD+
pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K/P192S
0.109
NAD+
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of acetaldehyde, at 25°C
0.28
NAD+
recombinant enzyme, pH and temperature not specified in the publication
0.29
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant T34Q/T39S/L43Q
0.362
NAD+
mutant enzyme F37G, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.366
NAD+
Q81X74, YP_027084
pH 8.6, temperature not specified in the publication
0.366
NAD+
Q81X74, YP_027084
at pH 8.5, temperature not specified in the publication
0.417
NAD+
mutant enzyme F37T, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.527
NAD+
mutant enzyme F37L, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.67
NAD+
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.75
NAD+
-
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
35
NAD+
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
100
NAD+
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.061
NADH
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
0.367
NADH
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
0.403
NADH
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
0.537
NADH
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
6
phosphate
pH 8.0, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
additional information
additional information
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activity depends non-linearly on protein concentration in the range 0.00003-0.003 mM. With increasing concentrations the apparently hyperbolic substrate saturation curves turn into sigmoidal ones
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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kinetic analysis and thermodynamics of purified euthermic and torpid enzyme
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additional information
additional information
kinetic isotope effects. The enzyme exhibits a kinetic mechanism in which first NAD+, then D-glyceraldehyde 3-phosphate bind to the active site resulting in the formation of a covalently bound thiohemiacetal intermediate. After oxidation of the thiohemiacetal and subsequent nucleotide exchange (NADH off, NAD+ on), the binding of inorganic phosphate and phosphorolysis yields the product 3-phospho-D-glyceroyl phosphate. Solvent and multiple kinetic isotope effects revealed that the first halfreaction is rate limiting and utilizes a step-wise mechanism for thiohemiacetal oxidation via a transient alkoxide to promote hydride transfer and thioester formation. steady-state kinetics
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additional information
additional information
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the enzyme presents allosteric positive cooperativity for substrates NAD+ and D-glyceraldehyde 3-phosphate, kinetic analysis, overview
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additional information
additional information
the mammalian enzyme shows negative cooperativity
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additional information
additional information
the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate
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additional information
additional information
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the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate
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additional information
additional information
the sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase exhibits strong positive cooperativity in coenzyme binding, kinetics, overview
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additional information
additional information
the sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase exhibits strong positive cooperativity in coenzyme binding, kinetics, overview
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additional information
additional information
enzyme kinetics, the recombinant enzyme exhibits about 6fold higher Km value toward 1,3-bisPGA compared to Ga3P. kcat in the way of Ga3P oxidation is about 5fold higher than in the opposite direction, thus resulting in a similar catalytic efficiency (kcat/Km) of the enzyme for the forward and the reverse reactions
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additional information
additional information
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enzyme kinetics, the recombinant enzyme exhibits about 6fold higher Km value toward 1,3-bisPGA compared to Ga3P. kcat in the way of Ga3P oxidation is about 5fold higher than in the opposite direction, thus resulting in a similar catalytic efficiency (kcat/Km) of the enzyme for the forward and the reverse reactions
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