Structural highlights
Function
[RHAB_ECO57] Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The enzyme L-rhamnulose kinase from Escherichia coli participates in the degradation pathway of L-rhamnose, a common natural deoxy-hexose. The structure of the enzyme in a ternary complex with its substrates ADP and L-rhamnulose has been determined at 1.55A resolution and refined to R(cryst)/R(free) values of 0.179/0.209. The result was compared with the lower resolution structure of a corresponding complex containing L-fructose instead of L-rhamnulose. In light of the two established sugar positions and conformations, a number of rare sugars have been modeled into the active center of L-rhamnulose kinase and the model structures have been compared with the known enzymatic phosphorylation rates. Rare sugars are of rising interest for the synthesis of bioactive compounds.
Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures.,Grueninger D, Schulz GE FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grueninger D, Schulz GE. Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures. FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582 doi:10.1016/j.febslet.2007.05.075
