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Crystal structures of thymidylate synthase mutant R166Q: Structural basis for the nearly complete loss of catalytic activity

โœ Scribed by Rogerio R. Sotelo-Mundo; Liming Changchien; Frank Maley; William R. Montfort


Book ID
102297634
Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
29 KB
Volume
20
Category
Article
ISSN
1095-6670

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Crystal structures of thymidylate syntha
โœ Rogerio R. Sotelo-Mundo; Liming Changchien; Frank Maley; William R. Montfort ๐Ÿ“‚ Article ๐Ÿ“… 2006 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 142 KB

Thymidylate synthase (TS) catalyzes the folate-dependent methylation of deoxyuridine monophosphate (dUMP) to form thymidine monophosphate (dTMP). We have investigated the role of invariant arginine 166, one of four arginines that contact the dUMP phosphate, using site-directed mutagenesis, X-ray cry