The isolation and identification of several individual enzymes has made it possible to attack the problem of their chemical structure. In the last few years it has been shown that urease (1), pepsin (2), trypsin (3), chymo-trypsin (4), probably pancreatic amylase (5) and rennin (24) are proteins, so that the general molecular structure of these enzymes is known. Enzymes have powerful catalytic properties, however, not possessed by ordinary proteins and therefore must possess characteristic chemical structures.Since the chemical properties of a molecule are not the sum of the properties of its component parts, the catalytic activity of an enzyme must be considered as a property of the whole molecule and cannot, strictly, be referred to one special group. It is frequently true, however, that a particular property of the molecule is dependent upon a particular group or arrangement of the atoms within the molecule; the magnitude of this property depends upon the structure of the whole molecule. Thus organic acids usually contain a carboxyl group but the strength of the group depends on the entire molecular configuration. In the case of proteins possessing peculiar properties the first question to arise is whether the molecule consists entirely of amino acids or whether it contains a prosthetic group; i.e., a compound not composed of amino acids. The peculiar properties of hemoglobin are ascribed to the presence of the prosthetic group, heine, which can easily be separated from the protein, globin. In this case the prosthetic group may be detected by its color. The yellow respiratory ferment of Warburg (6) is similar since again the prosthetic group is colored. In both these cases the characteristic properties are lost completely when the prosthetic group is separated from the rest of the molecule. The prosthetic group alone is therefore not responsible for the activity.