Differences in natural ligand and fluoropyrimidine binding to human thymidylate synthase identified by transient-state spectroscopic and continuous variation methods-Reference-Cited by-同舟云学术

Differences in natural ligand and fluoropyrimidine binding to human thymidylate synthase identified by transient-state spectroscopic and continuous variation methods

Published:2002-05 Issue:1 Volume:1597 Page:149-156
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Felder Takita,Dunlap R.Bruce,Dix Daniel,Spencer Trent

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference39 articles.

1. Separation, identification, and stoichiometry of the ternary complexes of thymidylate synthetase

2. Functional role of cysteine-146 in Escherichia coli thymidylate synthase.

3. Kinetics and thermodynamics of the interaction of 5-fluoro-2'-deoxyuridylate with thymidylate synthase

4. A kinetic study of thymidylate synthase from Lactobacillus casei.

5. Kinetic Scheme for Thymidylate Synthase from Escherichia coli: Determination from Measurements of Ligand Binding, Primary and Secondary Isotope Effects, and Pre-Steady-State Catalysis

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