Function
Glycerol kinase or ATP:glycerol 3-phosphotransferase (GK) phosphorylates glycerol forming glycerol 3-phosphate (G3P) using Mg-ATP as phosphate source. GK is a key enzyme in glycerol uptake and metabolism. Mutations of GK gene cause GK deficiency syndrome. PK is a multi-subunit allosteric enzyme. Its activity can be inhibited by fructose 1,6-bisphosphate (FBP) and by the glucose-specific phosphocarrier IIA(Glc). PK cofactor is a Zn atom which binds to the dimer[1].
Disease
GK Deficiency is an X-linked disease which has 3 forms: infantile, juvenile and adult[2]
Structural highlights
GK active site is located in a cleft between two domains[3].
- ↑ Kralova I, Rigden DJ, Opperdoes FR, Michels PA. Glycerol kinase of Trypanosoma brucei. Cloning, molecular characterization and mutagenesis. Eur J Biochem. 2000 Apr;267(8):2323-33. PMID:10759857
- ↑ Sehgal A, Stack J. Complex glycerol kinase deficiency: an X-linked disorder associated with adrenal hypoplasia congenita. Indian J Pediatr. 2005 Jan;72(1):67-9. PMID:15684452
- ↑ Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J. Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation. Biochemistry. 2004 Jan 20;43(2):362-73. PMID:14717590 doi:10.1021/bi034258o
