Glycerol kinase
glycerol kinase | |||||||||
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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 | ||||||||
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glycerol kinase | |
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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:
- 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, there were 20 structures of this protein in the PDB, most of which are homodimeric.
See also
External links
- Glycerol Kinase at the US 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.