Article
Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit.
Biochemistry - 18 Feb 1992
Guillou F, Liao M, Garcia-Espana A, Lusty C J
Abstract excerpt
The synthetase subunit of Escherichia coli carbamyl phosphate synthetase has two catalytic nucleotide-binding domains, one involved in the activation of HCO3- and the second in phosphorylation of carbamate. Here we show that a Glu841----Lys841 substitution in a putative ATP-binding domain located...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Amino Acid Sequence
- Bicarbonates
- Binding Sites
- Carbamoyl-Phosphate Synthase (Ammonia)
- Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
- Carbamyl Phosphate
- Catalysis
- Centrifugation, Density Gradient
- Cloning, Molecular
- Enzyme Activation
- Escherichia coli
- Kinetics