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Glycerol kinase

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glycerol kinase
glycerol kinase dimer, E.Coli
Identifiers
EC no.2.7.1.30
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
glycerol kinase
Identifiers
SymbolGK
NCBI gene2710
HGNC4289
OMIM300474
RefSeqNM_000167
UniProtP32189
Other data
EC number2.7.1.30
LocusChr. X p21.3
Search for
StructuresSwiss-model
DomainsInterPro

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:

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, there were 20 structures of this protein in the PDB, most of which are homodimeric.

See also

References

  1. ^ 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.