Rhamnulokinase
| Rhamnulokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.5 | ||||||||
| CAS no. | 9030-52-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Rhamnulokinase (EC 2.7.1.5) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from Escherichia coli converts the hexose sugar, L-rhamnulose (shown in its open-chain keto form) to L-rhamnulose 1-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The enzyme can also act on L-xylulose.[1] It is found in plants and its crystal structure has been determined.[2] The main role of the enzyme is to break down L-rhamnulose[3]
This enzyme is a transferase, specifically one 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.[4]
Structural studies
As of late 2007, four structures have been solved for this class of enzymes, with PDB accession codes PDB: 2CGJ, PDB: 2CGK, PDB: 2CGL, and PDB: 2UYT.[2]
References
- ↑ Wilson, DM; Ajl, S (March 1957). "Metabolism of L-rhamnose by Escherichia coli. II. The phosphorylation of L-rhamnulose". Journal of Bacteriology. 73 (3): 415–20. doi:10.1128/JB.73.3.415-420.1957. PMC 289814. PMID 13416205.
- 1 2 Grueninger, Dirk; Schulz, Georg E. (2006). "Structure and Reaction Mechanism of l-Rhamnulose Kinase from Escherichia coli". Journal of Molecular Biology. 359 (3): 787–797. doi:10.1016/j.jmb.2006.04.013. PMID 16674975.
- ↑ Grueninger, Dirk; Schulz, Georg E. (2007). "Substrate spectrum of l-rhamnulose kinase related to models derived from two ternary complex structures". FEBS Letters. 581 (16): 3127–3130. doi:10.1016/j.febslet.2007.05.075. PMID 17568582.
- ↑ Enzyme 2.7.1.5 at KEGG Pathway Database.
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