Tagatose-6-phosphate kinase
From Wikipedia the free encyclopedia
| 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[edit]
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[edit]
- 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.
