Article
Identification of a site necessary for allosteric regulation in T4-phage deoxycytidylate deaminase.
Biochemistry - 1 Mar 1994
Moore J T, Cieśla J M, Changchien L M, Maley G F, Maley F
Abstract excerpt
An allosteric inhibitor of dCMP deaminase, dTTP, forms a photolabile covalent bond with T4-phage dCMP deaminase in the presence of UV light at 254 nm. The importance of the methyl group in this process is supported by the findings that dUTP, also an allosteric inhibitor, does not photofix to the enzyme and that tritium is released from [methyl-3H dTTP during the course of the photofixation. That the bond formed...
Topics
- Alanine
- Allosteric Regulation
- Amino Acid Sequence
- Bacteriophage T4
- Base Sequence
- Chromatography, High Pressure Liquid
- DCMP Deaminase
- DNA, Viral
- Molecular Sequence Data
- Mutation
- Peptide Mapping