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

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For detailed information about glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), go to the full flat file.

Reaction

Synonyms

A2B2-GAPDH, A2B2-glyceraldehyde-3-phosphate dehydrogenase, A4 glyceraldehyde 3-phosphate dehydrogenase, A4-GAPDH, At1g12900, At3g26650, D-glyceraldehyde-3-phosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate phosphorylating), GapA, GapA-1, GAPA1, GAPA2, 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-G3PDH, 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+)

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

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

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Results	in table
53	Activating Compound
81	AA Sequence
5	Application
1	CAS Registry Number
25	Cloned(Commentary)
121	Cofactor
12	Crystallization (Commentary)
15	Disease/ Diagnostics
4	Expression
16	General Information
1	General Stability
2	IC50 Value
24	Inhibitors
7	Ki Value [mM]
117	KM Value [mM]
45	Localization
1	Metals/Ions
75	Molecular Weight [Da]
31	Natural Substrates/ Products (Substrates)
135	Organism
2	Oxidation Stability
6	Pathway
153	PDB ID
16	pH Optimum
1	pH Range
2	pI Value
37	Protein Variants
36	Purification (Commentary)
2	Reaction
15	Reaction Type
114	Reference
52	Source Tissue
45	Specific Activity [micromol/min/mg]
2	Storage Stability
80	Substrates and Products (Substrate)
51	Subunits
122	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
15	Temperature Stability [°C]
41	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.2.1.13 - glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in presence and absence of NADP+, to 2.6 A and 1.74 A resolution, respectively

Helicobacter pylori

-

695353

-

Methanothermus fervidus

-

11539, 287993

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

Saccharolobus solfataricus

P39460

721142

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

Saccharolobus solfataricus

P39460

720224

crystal structure of the non-regulatory A(4) isoform of glyceraldehyde-3-phosphate dehydrogenase complexed with NADP+

Spinacia oleracea

-

288002

hanging-drop vapour-diffusion method is used to grow crystals of recombinant A4-GAPDH, T33A and S188A A4-GAPDH mutants complexed with NADP+

Spinacia oleracea

P19866

656539

molecular docking of ferredoxin-NADP-reductase EC 1.18.1.2 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

Spinacia oleracea

P19866

688696

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)

Spinacia oleracea

P19866

689747

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

Spinacia oleracea

P19866

671163

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

Synechococcus elongatus PCC 7942 = FACHB-805

-

671164

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

Synechococcus sp.

-

671167