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Substrate spectrum of l ‐rhamnulose kinase related to models derived from two ternary complex structures
Author(s) -
Grueninger Dirk,
Schulz Georg E.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.05.075
Subject(s) - ternary complex , chemistry , enzyme , fructose , substrate (aquarium) , ternary operation , escherichia coli , biochemistry , stereochemistry , crystallography , biology , ecology , computer science , gene , programming language
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 1.55 Å 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.