Protein Family Models

GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold. [1]. 7578111. Crystal structure of glycosomal glyceraldehyde-3-phosphate. dehydrogenase from Leishmania mexicana: implications for. structure-based drug design and a new position for the inorganic. phosphate binding site.. Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG;. Biochemistry 1995;34:14975-14986. (from Pfam)

Date:

2024-08-14

GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold. [1]. 7578111. Crystal structure of glycosomal glyceraldehyde-3-phosphate. dehydrogenase from Leishmania mexicana: implications for. structure-based drug design and a new position for the inorganic. phosphate binding site.. Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG;. Biochemistry 1995;34:14975-14986. (from Pfam)

Date:

2024-08-14

This HMM represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, distinct NAD- and NADP- utilizing forms exist, typically being responsible for reactions in the anabolic and catabolic directions respectively [1].

Gene:

gap

Date:

2024-05-30

type I glyceraldehyde-3-phosphate dehydrogenase catalyzes the NAD-dependent oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

Date:

2024-05-21