PMID:7812717

Citation	Hardy, LW, Pacitti, DF and Nalivaika, E (1994) Use of a purified heterodimer to test negative cooperativity as the basis of substrate inactivation of Escherichia coli thymidylate synthase (Asn177-->Asp). Structure 2:833-8
Abstract	Thymidylate synthase (TS) converts deoxyuridylate to thymidylate, an essential DNA precursor. Replacement of Asn177 with aspartate (Asn177-->Asp) in Escherichia coli TS creates a novel ability to methylate 2'-deoxycytidylate (dCMP). The dCMP-methylase activity of TS(Asn177-->Asp) is transiently inactivated by reaction with deoxyuridylate and methylene-tetrahydrofolate, the methyl donor. We have tested the possibility that the inactivation is due to negative cooperativity, created in the TS dimer by the Asn177-->Asp mutation.
Links	PubMed
Keywords	Amino Acid Sequence; Asparagine; Aspartic Acid; Binding Sites; Cloning, Molecular; Escherichia coli/enzymology; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Protein Structure, Secondary; Recombinant Proteins/antagonists & inhibitors; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Thymidylate Synthase/antagonists & inhibitors; Thymidylate Synthase/chemistry; Thymidylate Synthase/metabolism
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