Glycerol kinase
| glycerol kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:1glf.jpg 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, encoded by the gene GK, 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 3-phosphate
- Converted from glycerol 3-phosphate to dihydroxyacetone phosphate (DHAP) via glycerol 3-phosphate dehydrogenase. DHAP 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 US National Library of Medicine Medical Subject Headings (MeSH)
References
- ↑ Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
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