Glycerol kinase
| glycerol kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 glycerol kinase dimer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.30 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| glycerol kinase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | GK | ||||||
| NCBI gene | 2710 | ||||||
| HGNC | 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 involved in triglycerides and glycerophospholipids synthesis. The enzyme catalyses the chemical reaction:
-3-(phosphonatooxy)propane-1,2-diol.svg)
The enzyme characterised from liver converts glycerol to (R)-glyceryl 1-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2]
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.[citation needed]
Enzyme regulation
[edit]This protein may use the morpheein model of allosteric regulation.[3]
Structure
[edit]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.
External links
[edit]- Glycerol+Kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
References
[edit]- ↑ Bublitz, C.; Kennedy, E.P. (1955). "Synthesis of phosphatides in isolated mitochondria. III. The enzymatic phosphorylation of glycerol" (pdf). Journal of Biological Chemistry. 211: 951–961. PMID 13221600.
- ↑ Enzyme 2.7.1.30 at KEGG Pathway Database.
- ↑ 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.
 | This EC 2.7 enzyme-related article is a stub. You can help Wikipedia by adding missing information. |
