Publication Abstract from PubMed
Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.
Structure of the Y94F mutant of Escherichia coli thymidylate synthase.,Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:16946460[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
