Journal
IUBMB LIFE
Volume 53, Issue 2, Pages 85-98Publisher
WILEY
DOI: 10.1080/15216540211468
Keywords
acetoacetate decarboxylase; bacteriorhodopsin; cysteine protease; glycosidase; serine protease; thioredoxin
Categories
Ask authors/readers for more resources
In protein and RNA macromolecules, only a limited number of different side-chain chemical groups are available to function as catalysts. The myriad of enzyme-catalyzed reactions results from the ability of most of these groups to function either as nucleophilic, electrophilic, or general acid-base catalysts, and the key to their adapted chemical function lies in their states of protonation. Ionization is determined by the intrinsic pK(a) of the group and the microenvironment created around the group by the protein or RNA structure, which perturbs its intrinsic pK(a) to its functional or apparent pK(a). These pK(a) shifts result from interactions of the catalytic group with other fully or partially charged groups as well as the polarity or dielectric of the medium that surrounds it. The electrostatic interactions between ionizable groups found on the surface of macromolecules are weak and cause only slight pK(a) perturbations (<2 units). The sum of many of these weak electrostatic interactions helps contribute to the stability of native or folded macromolecules and their ligand complexes. However, the pK(a) values of catalytic groups that are found in the active sites of numerous enzymes are significantly more perturbed (>2 units) and are the subject of this review. The magnitudes of these pK(a) perturbations are analyzed with respect to the structural details of the active-site microenvironment and the energetics of the reactions that they catalyze.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available