Tagatose kinase
| tagatose kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.101 | ||||||||
| 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 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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2FIQ.
References
[edit]- Szumiøo T (August 1981). "A novel enzyme, tagatose kinase, from Mycobacterium butyricum". Biochimica et Biophysica Acta (BBA) - Enzymology. 660 (2): 366–70. doi:10.1016/0005-2744(81)90182-0. PMID 6269638.
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