Uroporphyrinogen decarboxylation as a benchmark for the catalytic proficiency of enzymes.

ABSTRACT: The magnitude of an enzyme's affinity for the altered substrate in the transition state exceeds its affinity for the substrate in the ground state by a factor matching the rate enhancement that the enzyme produces. Particularly remarkable are those enzymes that act as simple protein catalysts, without the assistance of metals or other cofactors. To determine the extent to which one such enzyme, human uroporphyrinogen decarboxylase, enhances the rate of substrate decarboxylation, we examined the rate of spontaneous decarboxylation of pyrrolyl-3-acetate. Extrapolation of first-order rate constants measured at elevated temperatures indicates that this reaction proceeds with a half-life of 2.3 x 10(9) years at 25 degrees C in the absence of enzyme. This enzyme shows no significant homology wit

SUBMITTER: Lewis CA 

PROVIDER: S-EPMC2582308 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature