Tagatose kinase
| tagatose kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.101 | ||||||||
| CAS number | 39434-00-9 | ||||||||
| 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 tagatose kinase (EC 2.7.1.101) is an enzyme that catalyzes the chemical reaction
- ATP + D-tagatose ADP + D-tagatose 6-phosphate
Thus, the two substrates of this enzyme are ATP and D-tagatose, whereas its two products are ADP and D-tagatose 6-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:D-tagatose 6-phosphotransferase. Other names in common use include tagatose 6-phosphate kinase (phosphorylating), D-tagatose 6-phosphate kinase, and tagatose-6-phosphate kinase. This enzyme participates in galactose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2FIQ.
References
- Szumioo T (1981). "A novel enzyme, tagatose kinase, from Mycobacterium butyricum". Biochim. Biophys. Acta. 660 (2): 366–70. doi:10.1016/0005-2744(81)90182-0. PMID 6269638.