Tagatose-6-phosphate kinase
| tagatose-6-phosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.144 | ||||||||
| CAS no. | 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-6-phosphate kinase (EC 2.7.1.144) is an enzyme that catalyzes the chemical reaction
- ATP + D-tagatose 6-phosphate ADP + D-tagatose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and D-tagatose 6-phosphate, whereas its two products are ADP and D-tagatose 1,6-bisphosphate.
This enzyme belongs to the phosphofructokinase B (PfkB) or Ribokinase family of sugar kinases, 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-phosphate 1-phosphotransferase. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs and their enzymatic activity generally shows a dependence on the presence of pentavalent ions. Pentavalent ions dependency is a conserved property of adenosine kinase from diverse sources: identification of a novel motif implicated in phosphate and magnesium ion binding and substrate inhibition. Biochemistry 2002, 41: 4059-4069.</ref> This enzyme participates in galactose metabolism.
Structural studies
As of late 2007, five structures have been solved for this class of enzymes, with PDB accession codes 2AWD, 2F02, 2JG1, 2JGV, and 2Q5R.
References
- Nobelmann B, Lengeler JW (1995). "Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli". Biochim. Biophys. Acta. 1262 (1): 69–72. doi:10.1016/0167-4781(95)00053-j. PMID 7772602.
