Glycerol kinase

glycerol kinase

glycerol kinase dimer, E.Coli
Identifiers
EC number 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
Entrez 2710
HUGO 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:

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 3298769Freely accessible. PMID 22182754.


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