Glyceraldehyde-3-Phosphate Dehydrogenase

Glyceraldehyde-3-Phosphate DehydrogenaseGlyceraldehyde-3-Phosphate Dehydrogenase

spinqualitylabelsall models PDB ID 3gpd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
3gpd, resolution 3.50Å ()
Ligands:	,
Activity:	Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12
Structural annotation: Resources: CATH : 3Gpdg02, 3Gpdg01, 3Gpdr01, 3Gpdr02 InterPro : Ipr000173, Ipr006424 Pfam : PF00044, PF02800 SCOP : d3gpdg1, d3gpdg2, d3gpdr1, d3gpdr2 UniProt : P04406
Functional annotation: Cellular component: cytoplasm Biological process: glycolysis glucose metabolic process Molecular function: glyceraldehyde-3-phosphate dehydrogenase activity oxidoreductase activity protein binding glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity NAD binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a very important enzyme in the production of energy. This enzyme catalyzes the sixth step in the process of breaking down glucose into energy, also known as glycolysis. Though this is its main function, GAPDH has been shown to perform other functions including transcription activation, initiation of apoptosis, and ER to Golgi apparatus vesicle transportation. However, this page will focus on GAPDH’s role in glysolysis. GAPDH most commonly exists as what looks to be a dimer. Interesting though, the two monomers of the enzyme are not exactly the same. While one side consists only of parallel and antiparallel beta-sheets, the other monomer is made up of both . This is consistent with the following SCOP information:

Class: Alpha and beta proteins (a/b)

Fold: NAD(P)-binding Rossmann-fold domains

Superfamily: NAD(P)-binding Rossmann-fold domains

Family: Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminus domain

Protein: Glyceraldehyde-3-phosphate dehydrogenase

Species: Human

The specific reaction that GAPDH catalyzes is shown below:

The mechanism of the glycolysis reaction is fairly straight forward. After the aldehyde enters the active site, the sulfhydryl group from attacks the nucleophilic carbon to form a thiohemiacetal. This intermediate undergoes oxidation due to a hydride transfer to a nearby NAD+ forming a thioester. From here, a phosphate group enters and attacks the same carbonyl while at the same time it is separated from the cystine by the protonated group. This produces the desired 1,3-bisphosphoglycerate.