Enzymes
A substrate binds an active site whose shape and chemical properties stabilize the transition state. Temperature, pH, substrate concentration, and inhibitors influence rate. A competitive inhibitor binds the active site; increasing substrate can reduce its effect. Allosteric binding alters activity at another site. Denaturation disrupts the structure needed for function, without normally breaking the primary peptide backbone.
If a competitive inhibitor is added, more substrate can restore a high rate by competing for active sites.
A catalyst does not make an energetically unfavorable reaction favorable.