active site 1 the general region of an enzyme molecule containing the catalytic residues identified with the binding and reaction of substrate( s). It includes those amino-acid residues that are, in the enzyme– substrate complex, either contact amino acids, i.e. those that at some point are only one bond distance removed from some point of
acetate–CoA ligase EC 6.2.1.1; systematic name: acetate:CoA ligase (AMP-forming); other names: acetyl–CoA synthetase; acyl-activating enzyme; acetate thiokinase; acetyl-activating enzyme. An enzyme that catalyses a reaction between ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl-CoA. It is an important enzyme in organisms (e.g. Escherichia coli, many fungi, protozoans, algae) that utilize acetate as a
An enzyme that has two structurally distinct forms, one of which is active and the other inactive. In the active form, the quaternary structure of the enzyme is such that a substrate can interact with the enzyme at the active site. The conformation of the substrate-binding site becomes altered in the inactive form and interaction