glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

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Word Map on EC


D-glyceraldehyde 3-phosphate
3-phospho-D-glyceroyl phosphate


A2B2-GAPDH, A2B2-glyceraldehyde-3-phosphate dehydrogenase, A4 glyceraldehyde 3-phosphate dehydrogenase, A4-GAPDH, D-glyceraldehyde-3-phosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate phosphorylating), GapA, GapA-1, GapB, GAPC, GAPD, GAPDH, GAPDH (A4), glyceraldehyde 3-phosphate dehydrogenase (NADP), glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate phosphorylating), glyceraldehyde-3-dehydrogenase, glyceraldehyde-3-P dehydrogenase, glyceraldehyde-3-phosphate dehhydrogenase (NADP+) (phoshphorylating), glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NADP+), glyceraldehyde-P dehydrogenase, GraP-DH, NAD(P)-GAPDH, NADP(H)-glyceraldehyde-3-phosphate dehydrogenase, NADP+-dependent G-3-P dehydrogenase, NADP+-dependent gapB, NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase, NADP+-GAPDH, NADP-dependent GAPDH, NADP-dependent glyceradehdye-3-phosphate dehydrogenase, NADP-dependent glyceraldehyde 3-phosphate dehydrogenase, NADP-dependent glyceraldehyde phosphate dehydrogenase, NADP-dependent glyceraldehydephosphate dehydrogenase, NADP-GAPDH, NADP-glyceraldehyde phosphate dehydrogenase, NADP-glyceraldehyde-3-phosphate dehydrogenase, NADP-GPD, NADP-triose phosphate dehydrogenase, NADPH-D-GA3P, NADPH-glyceraldehyde-3-phosphate dehydrogenase, NAPD-linked glyceraldehyde-3-P dehydrogenase, Ov-GAPDH, phosphorylating GAP dehydrogenase, phosphorylating glyceraldehyde-3-phosphate dehydrogenase, photosynthetic GAPDH, SSO0528, triosephosphate dehydrogenase (NADP+)


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


Crystallization on EC - glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

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in presence and absence of NADP+, to 2.6 A and 1.74 A resolution, respectively
crystallized from ammonium sulfate to produce crystals that diffract to 2.4 A with a space group of P4(3)2(1)2 or P4(1)2(1)2
determination of the crystal structure of the apoenzyme by multiple isomorphous replacement at 2.05 A resolution, hanging drop technique. The crystals belong to space group P4(1)2(1)2 or its enantiomorph with cell dimensions a = b = 102.3 A, c = 181.6 A, which contract upon cryocooling at 100 K to a = b = 101.6 A, c = 179.9 A. The asymmetric unit contains two subunits with a molecular mass of 37611 Da
crystal structure of the non-regulatory A(4) isoform of glyceraldehyde-3-phosphate dehydrogenase complexed with NADP+
hanging-drop vapour-diffusion method is used to grow crystals of recombinant A4-GAPDH, T33A and S188A A4-GAPDH mutants complexed with NADP+
molecular docking of ferredoxin-NADP-reductase EC and GAPD. enzymes are able to form at least two different complexes, one involving a single GAPD monomer and an ferredoxin-NADP-reductase monomer or dimer. The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer or dimer. Ferredoxin is able to interact with FNR in either complex
sitting drop vapour diffusion method with 2.0-2.5 M or 1.5-1.2 M ammonium sulfate and 0.1 M potassium phosphate (pH 7.0-8.0)
two crystal forms of the A4-GAPDH isoform are used to solve the structure of the apo form to a resolution of 3.0 A
the structure of NADP-dependent GAPDH in complex with NADP is solved by molecular replacement and refined to an R factor of 19.1% and a free R factor of 24% at 2.5 A resolution
the crystal structure of apo-glyceraldehyde-3-phosphate dehydrogenase is solved by molecular replacement and refined to an R of 21.7% and Rfree of 27.5% at 2.9 A resolution