Rhamnulokinase () 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. It is found in plants and its crystal structure has been determined. The main role of the enzyme is to break down L-rhamnulose
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.
Structural studies As of late 2007, four structures have been solved for this class of enzymes, with PDB accession codes , , , and .
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