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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

Reaction

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

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

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

Temperature Stability

Temperature Stability on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
109
-
transition temperature
15 - 60
-
pre-incubation for 10 min at temperatures varying between 15°C and 30°C does not irreversibly affect the enzyme activity, thermal inactivation occurs above 35°C and results in total activity loss at 60°C
15 - 70
-
pre-incubation for 10 min at temperatures varying between 20 and 32°C does not irreversibly affect the enzyme activity, thermal inactivation occurs above 35°C and results in total activity loss at 70°C
27
-
pH 8.5, half-life: 2 days
34 - 55
-
long topor GAPDH is significantly less susceptible to thermal denaturation as compared to euthermic GAPDH, with 45°C or 55°C being required to cause a significant decrease in long topor GAPDH enzyme activity as compared to 35-45°C for euthermic GAPDH. Long topor GAPDH displays a significantly higher thermal melting point of 56.1°C as compared to the euthermic GAPDH Tm of 54.7°C
35
-
30 min, stable up to
43
-
30 min, 50% inactivation, irreversible
45
-
GAPDH is inactivated at 45°C, alpha-crystallin accelerates the thermal inactivation of GAPDH at 45°C and reduces thermostability of the enzyme, while GroEL does not affect thermal inactivation and denaturation of GAPDH
58
-
pH 7.0, 20 min, 50% inactivation
60
-
pH 7.5, 30 min, about 40% loss of activity
60 - 70
-
retains structural integrity and enzymatic activity up to
61.6
-
thermal unfolding of GAPDH is characterized by sharp thermal transition with a maximum at 61.6°C, GAPDH stability is diminished in the presence of alpha-crystallin (0.4 mg/ml)
62
-
maximum of thermal transition peak of tetrameric form of mutant apoenzyme N313T
63.2
enzyme without NAD+
65
purified recombinant His-tagged enzyme, inactivation
65.4
-
maximum of thermal transition peak of dimeric mutant apoenzyme Y46G/S48G
65.5
-
maximum of thermal transition peak of dimeric mutant apoenzyme Y46G/R52G
66
-
melting temperature at 66°C
68.4
-
maximum of thermal transition peak of tetrameric mutant apoenzyme Y283V
70
-
loss of activity within a few min
70.3
-
maximum of thermal transition peak of tetrameric mutant apoenzyme D283G
70.7
-
maximum of thermal transition peak of tetrameric mutant apoenzyme W310F
71
-
maximum of thermal transition peak of dimeric mutant apoenzyme D282G
73.5
-
maximum of thermal transition peak of dimeric mutant apoenzyme Y283V
78.4
NAD+-bound enzyme
78.5
-
maximum of thermal transition peak of tetrameric form of wild-type apoenzyme
80 - 102
-
the enzyme is fully active at temperatures near 80°C but has very low activity at room temperature, the melting temperature is at 102°C
85
-
pH 8.5, protein concentration 2.1 mg/ml, 10 min, stable
additional information