Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis.
Glycerol kinase catalyzes the transfer of a phosphate from ATP to glycerol thus forming glycerol phosphate (ATP + glycerol <=> ADP + sn-glycerol 3-phosphate). Adipocytes lack glycerol kinase so they cannot metabolize the glycerol produced during triacyl glycerol degradation. This glycerol is instead shuttled to the liver via the blood where it is:
- phosphorylated by glycerol kinase to glycerol phosphate
- converted to DHAP (dihydroxyacetone phosphate) which can participate in glycolysis or gluconeogenesis.
This protein may use the morpheein model of allosteric regulation. 
Glycerol Kinase (alternative name, ATP:glycerol 3-phosphotransferase or Glycerokinase) adopts a ribonuclease H-like fold consisting of an alpha-beta 2-layer sandwich of CATH family 3.30.420.40. As of March 2010 , there were 20 structures of this protein in the PDB, most of which are homodimeric.
- Biochemistry, Champe, P.C., Harvey, R.A., Ferrier, D.R., 3rd ed., 2005.
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