Article
Crystal structures of a marginally active thymidylate synthase mutant, Arg 126-->Glu.
Protein science : a publication of the Protein Society - 1 Dec 1997
Strop P, Changchien L, Maley F, Montfort W R
Abstract excerpt
Thymidylate synthase (TS) is a long-standing target for anticancer drugs and is of interest for its rich mechanistic features. The enzyme catalyzes the conversion of dUMP to dTMP using the co-enzyme methylenetetrahydrofolate, and is perhaps the best studied of enzymes that catalyze carbon-carbon...
Topics
- Antineoplastic Agents
- Arginine
- Binding Sites
- Catalysis
- Crystallization
- Crystallography, X-Ray
- Deoxyuracil Nucleotides
- Dimerization
- Folic Acid
- Folic Acid Antagonists
- Glutamic Acid
- Hydrogen Bonding
- Kinetics
- Models, Molecular
- Molecular Structure
- Mutation
- Phosphates
- Quinazolines