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Literature summary extracted from

  • Shen, Y.Q.; Song, S.Y.; Lin, Z.J.
    Structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues (2002), Acta Crystallogr. Sect. D, 58, 1287-1297.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.12 structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues ADPribose and thio-NAD+. The crystals of both GAPDH complexes belong to the same space group C2 as holeenzyme or apoenzyme, but with different unit-cell parameters Panulirus versicolor

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.12 ADP-ribose coenzyme analogue with a non-cooperative behaviour of binding, is a potent competitive inhibitor Panulirus versicolor

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Panulirus versicolor P56649
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.12 tail muscle
-
 Panulirus versicolor
-

Synonyms

EC Number Synonyms Comment Organism
1.2.1.12 D-glyceraldehyde-3-phosphate dehydrogenase
-
 Panulirus versicolor
1.2.1.12 GAPDH
-
 Panulirus versicolor

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 thio-NAD+ the coenzyme analogue binds in a non-productive manner, resulting in a disordered thionicotinamide ring and rearranged active-site residues, effective as substrate to replace NAD+ Panulirus versicolor