Tagatose-6-phosphate kinase

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 ${\displaystyle \rightleftharpoons }$ ADP + D-tagatose 1,6-bisphosphate

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
Search PMC articles PubMed articles NCBI proteins

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.