Correlation of Structure and Function in Enzyme Action

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Abstract
This brief survey of some of the highlights in the correlation of enzyme structure and function indicates the considerable progress that has been made and also the important problems that are still unsolved. Protein reagents and x-ray crystallography are among the powerful tools which have changed our description of proteins from cumulus-cloud-type drawings to detailed pictures involving the precise positioning of atoms. Physical chemistry has also proceeded to a stage in which catalysis can be explained in terms of acids and bases, electron donors and acceptors. Finally, in the modification studies a correlation is beginning to be made between specific amino acid residues in the protein and their possible roles in polarizing electrons in the substrate molecules. Of the conclusions already obtained, one of the most important is that the concept of a small "active site," which was deduced from simple geometric considerations, seems to be strongly supported by the modification studies. Not only are vast regions of the protein unnecessary for enzyme action but amino acid residues, one or two residues away from essential residues, can be modified with little or no change in the enzyme action.