Download MendeleySubstrate Spectrum of L-Rhamnulose Kinase Related to Models Derived from Two Ternary Complex Structures.
Grueninger, D., Schulz, G.E.(2007) FEBS Lett 581: 3127
- PubMed: 17568582
- DOI: https://doi.org/10.1016/j.febslet.2007.05.075
- Primary Citation of Related Structures:
2UYT - PubMed Abstract:
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.
Organizational Affiliation:
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, 79104 Freiburg im Breisgau, Germany.
