Thymidylate synthetase: Fluorine-19 nmr characterization of the active site peptide covalently bound to 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate-Reference-Cited by-同舟云学术

Thymidylate synthetase: Fluorine-19 nmr characterization of the active site peptide covalently bound to 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate

Published:1976-09 Issue:2 Volume:72 Page:404-410
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

James Thomas L.,Pogolotti Alfonso L.,Ivanetich Kathryn M.,Wataya Yusuke,Lam Stella S.M.,Santi Daniel V.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference18 articles.

1. Model studies of thymidylate synthetase. Neighboring-group facilitation of electrophilic substitution reactions of uracil furanosides

2. Model studies of thymidylate synthetase. Intramolecular catalysis of 5-hydrogen exchange and 5-hydroxymethylation of 1-substituted uracils

3. Model studies of the thymidylate synthetase reaction. Nucleophilic displacement of 5-p-nitrophenoxymethyluracils

4. Mechanism of interaction of thymidylate synthetase with 5-fluorodeoxyuridylate

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