Purification and amino acid analysis of an active site peptide from thymidylate synthetase containing covalently bound 5-fluoro-2′-deoxyuridylate and …
H Sommer, DV Santi - Biochemical and biophysical research …, 1974 - Elsevier
H Sommer, DV Santi
Biochemical and biophysical research communications, 1974•ElsevierThymidylate synthetase forms a complex with 5-fluoro-2′-deoxyuridylate and 5, 10-
methylenetetrahydrofolate in which a nucleophile of the enzyme is covalently attached to the
6-position of the nucleotide. Treatment of the complex with Pronase provides a small peptide
to which both the nucleotide and cofactor are covalently attached. From amino acid analysis,
it may be deduced that the amino acid which is covalently attached to 5-fluoro-2′-
deoxyuridylate is threonine or histidine. Implications with regard to catalysis are discussed.
methylenetetrahydrofolate in which a nucleophile of the enzyme is covalently attached to the
6-position of the nucleotide. Treatment of the complex with Pronase provides a small peptide
to which both the nucleotide and cofactor are covalently attached. From amino acid analysis,
it may be deduced that the amino acid which is covalently attached to 5-fluoro-2′-
deoxyuridylate is threonine or histidine. Implications with regard to catalysis are discussed.
Abstract
Thymidylate synthetase forms a complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate in which a nucleophile of the enzyme is covalently attached to the 6-position of the nucleotide. Treatment of the complex with Pronase provides a small peptide to which both the nucleotide and cofactor are covalently attached. From amino acid analysis, it may be deduced that the amino acid which is covalently attached to 5-fluoro-2′-deoxyuridylate is threonine or histidine. Implications with regard to catalysis are discussed.
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