The role of lysine residues 297 and 306 in nucleoside triphosphate regulation of E. coli CTP synthase: inactivation by 2',3'-dialdehyde ATP and mutational analyses.

Abstract excerpt

Cytidine 5'-triphosphate synthase (CTPS) catalyzes the ATP-dependent formation of CTP from UTP using either NH3 or L-glutamine as the source of nitrogen. To identify the location of the ATP-binding site within the primary structure of E. coli CTPS, we used the affinity label 2',3'-dialdehyde adenosine 5'-triphosphate (oATP). oATP irreversibly inactivated CTPS in a first-order, time-dependent manner while ATP...

Topics

• Adenosine Triphosphate
• Amino Acid Sequence
• Binding Sites
• Carbon-Nitrogen Ligases
• Cytidine Triphosphate
• DNA Mutational Analysis
• Escherichia coli
• Kinetics
• Lysine
• Molecular Sequence Data
• Mutation
• Protein Conformation