Glycerate kinase

From Proteopedia

spinqualitylabelsall models Glycerate kinase dimer complex with sulfate ions (PDB code 1to6). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Glycerate kinase (GK) catalyzes the conversion of ATP + glycerate to ADP + 3-phospho-glycerate. GK participates in the metabolic pathways of serine/glycine/threonine, glycolipid and glyoxylate-dicarboxylate. GK is the last step in the pathway which starts with glucose and ends with 2-phosphoglycerate[1]. Disease Mutation in GK is the cause of inherited D-glyceric acidemia (D-glyceric aciduria)[2].

3D Structures of glycerate kinase

Updated on 03-March-2020

1to6 – GK – Neisseria meningitides
2b8n – GK – Thermotoga maritima
1x3l – GK – Pyrococcus horikoshii
3cwc – GK – Salmonella enterica
6ckg – GK – Cryptococcus neoformans

References

1. ↑ Doughty CC, Hayashi JA, Guenther HL. Purification and properties of D-glycerate 3-kinase from Escherichia coli. J Biol Chem. 1966 Feb 10;241(3):568-72. PMID:5325263
2. ↑ Sass JO, Fischer K, Wang R, Christensen E, Scholl-Burgi S, Chang R, Kapelari K, Walter M. D-glyceric aciduria is caused by genetic deficiency of D-glycerate kinase (GLYCTK). Hum Mutat. 2010 Dec;31(12):1280-5. doi: 10.1002/humu.21375. Epub 2010 Nov 9. PMID:20949620 doi:http://dx.doi.org/10.1002/humu.21375