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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)

Metals Ions

Metals Ions on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
0.045 M, 10fold activation
KCl
-
exhibits its highest activity in 2 mol/l KCl at 45°C
Na2SO4
-
up to 5fold activation
NH4Cl
RbCl
-
activity is enhanced by increasing concentrations of the salt. Optimum activity in 3 M RbCl
Zn
-
enzyme form E8.5 contains 0.64 gatoms of zinc per mol of enzyme, enzyme form E9.0 contain 2.76 gatom of zinc per mol of enzyme
additional information
the apo subunit D of the enzyme's crystal structure contains three sulfate ions labelled SUL1, SUL2 and SUL3. SUL1 binds to Ser151, Thr212 and Gly213 by hydrogen bonds. The location of SUL2 is similar to the position of the sulfate ion in subunit A, and the residues to which SUL2 binds by hydrogen bonds are identical to those in subunit A, including Thr182, Arg199 and Arg235. In addition, SUL3 is hydrogen-bonded to the backbone amino group of Arg12. The anion-binding sites located by sulfate ions in our structure could naturally be occupied by phosphate ions