Glycerol kinase

Revision as of 02:11, 25 August 2017 by en>DrMoof (I fixed a typo. "Glycerol 3-Phosphate Dehydrogenae" to "Glycerol 3-Phosphate Dehydrogenase")
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glycerol kinase
File:1glf.jpg
glycerol kinase dimer, E.Coli
Identifiers
EC number2.7.1.30
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
glycerol kinase
Identifiers
SymbolGK
Entrez2710
HUGO4289
OMIM300474
RefSeqNM_000167
UniProtP32189
Other data
EC number2.7.1.30
LocusChr. 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:

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

External links

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.