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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)

General Stability

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

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1% SDS, fully active
-
5 M, 0°C, 1 h, complete loss of activity, 5 mM NAD+ protects
-
5.0 M guanidine-HCl, rapid and irreversible inactivation at 30°C
-
8 M urea, 30°C, 0.05 M phosphate buffer, 50% loss of activity after 1 min
-
8 M urea, 40% inactivation
-
8.0 M urea, unusually resistant at 30°C, 40°C and 50°C. Rapid inactivation at 55°C and at 60°C
-
acetylleucine chloromethyl ketone binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196
-
alpha-crystallin accelerates the thermal inactivation of GAPDH, while GroEL does not affect thermal inactivation and denaturation of GAPDH
-
binding to erythrocyte membranes stabilizes the enzyme at 4°C
-
freezing in liquid nitrogen results in partial loss of activity
-
higher salt (300 mM NaCl) concentrations stabilizes the tetrameric state. Also binding of the cofactor NAD+ causes a conformational rearrangement in the enzyme structure, leading to the stabilization of the enzyme
it cannot be stabilized with sorbitol, glucose, polyethylene glycol 400, beta-alanine, glycine or glycerol
-
rapid loss of activity without protection by a thiol
-
repeated freezing and thawing brings about 10-20% inactivation
-
stable for many days in all buffers, containing more than 2 mol/l salt
-
very stable in 4 M KCl. Inactivated within 12 h in 0.5 M KCl, 50 mM Tris-HCl, pH 8.0, at 25°C
-