Rhamnulokinase
| rhamnulokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.5 | ||||||||
| CAS number | 9030-52-8 | ||||||||
| 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 rhamnulokinase (EC 2.7.1.5) is an enzyme that catalyzes the chemical reaction
- ATP + L-rhamnulose ADP + L-rhamnulose 1-phosphate
Thus, the two substrates of this enzyme are ATP and L-rhamnulose, whereas its two products are ADP and L-rhamnulose 1-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:L-rhamnulose 1-phosphotransferase. Other names in common use include RhuK, rhamnulokinase (phosphorylating), L-rhamnulokinase, L-rhamnulose kinase, and rhamnulose kinase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes by Grueninger and Schulz with PDB accession codes 2CGJ, 2CGK, 2CGL, and 2UYT.
References
- Wilson DM; Ajl S (1957). "METABOLISM OF l-RHAMNOSE BY ESCHERICHIA COLI: II. The Phosphorylation of l-Rhamnulose". J. Bacteriol. 73 (3): 415&ndash, 420. PMC 289814. PMID 13416205.
- D.Grueninger and G.E.Schulz (2006). Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli.. J. Mol. Biol., 359, 787-797.
- D.Grueninger and G.E.Schulz (2007). Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures.. FEBS Lett, 581, 3127-3130.