Biology:Glycerone kinase
| glycerone kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.29 | ||||||||
| CAS number | 9027-47-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a glycerone kinase (EC 2.7.1.29) is an enzyme that catalyzes the chemical reaction
- ATP + glycerone [math]\displaystyle{ \rightleftharpoons }[/math] ADP + glycerone phosphate
Thus, the two substrates of this enzyme are ATP and glycerone, whereas its two products are ADP and glycerone phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:glycerone phosphotransferase. Other names in common use include dihydroxyacetone kinase, acetol kinase, and acetol kinase (phosphorylating). This enzyme participates in glycerolipid metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1OI2, 1OI3, 1UN8, 1UN9, 1UOD, and 1UOE.
References
- "Phosphorylation of acetol by homogenates of rat liver". Fed. Proc. 16: 245–246. 1957.
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