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Literature summary for 1.2.1.12 extracted from

  • Gaston, D.; Roger, A.
    Functional divergence and convergent evolution in the plastid-targeted glyceraldehyde-3-Phosphate dehydrogenases of diverse eukaryotic algae (2013), PLoS ONE, 8, e70396 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.12

Crystallization (Commentary)

Crystallization (Comment) Organism
quaternary structure of the GAPDH A2B2 heterotetramer, PDB ID 2PKQ, from Spinacia oleracea, crystallographic subunits O (GapB) and R (GapA) Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Spinacia oleracea 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Spinacia oleracea
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Spinacia oleracea P19866
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Spinacia oleracea 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r

Subunits

Subunits Comment Organism
homotetramer functional GAPDH is a homotetramer, with each monomer composed of two domains: the N-terminal coenzyme binding domain and the C-terminal catalytic domain. The catalytic domain contains the Ps and Pi sites, which bind the C(3) phosphate of the substrate and the inorganic phosphate ion, respectively, during the phosphorylation step carried out by the enzyme. The S-loop folds over in close proximity to the bound cofactor, modelling Spinacia oleracea

Synonyms

Synonyms Comment Organism
GAPDH
-
 Spinacia oleracea
glyceraldehyde-3-phosphate dehydrogenase
-
 Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Spinacia oleracea
NADH
-
 Spinacia oleracea

General Information

General Information Comment Organism
evolution convergent evolution in GapA/B and GapC1, plastid GapC1 and GapA represent two independent cases of functional divergence and adaptations to the Calvin cycle entailing a shift in subcellular targeting and a shift in binding preference from NAD+ to NADPH. Comparisons between GapA sequences and cytosolic GAPDH and GapC1 and cytosolic GAPDH sequences (Gap2, GapA, GapB, or GapC1) to identify possible functionally divergent sites, homology modeling, phylogenetic tree, detailed overview Spinacia oleracea
physiological function glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme of the glycolytic pathway, reversibly catalyzing the sixth step of glycolysis and concurrently reducing the coenzyme NAD+ to NADH Spinacia oleracea