Glycerol kinase
| glycerol kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 glycerol kinase dimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.30 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| glycerol kinase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | GK | ||||||
| NCBI gene | 2710 | ||||||
| HGNC | 4289 | ||||||
| OMIM | 300474 | ||||||
| RefSeq | NM_000167 | ||||||
| UniProt | P32189 | ||||||
| Other data | |||||||
| EC number | 2.7.1.30 | ||||||
| Locus | Chr. X p21.3 | ||||||
| |||||||
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 3-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 dihydroxyacetone phosphate (DHAP) which can participate in glycolysis or gluconeogenesis.
Enzyme regulation
This protein may use the morpheein model of allosteric regulation.[1]
Structure
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[update], there were 20 structures of this protein in the PDB, most of which are homodimeric.
See also
External links
- Glycerol+Kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
References
- ^ T. Selwood; E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
- Biochemistry, Champe, P.C., Harvey, R.A., Ferrier, D.R., 3rd ed., 2005.