Abstract
Two fractions containing NADPH-enoyl CoA reductase activities were isolated from crude extracts of Candida albicans. One fraction (Type-I) having larger molecular weight utilizes 5-hydroxyundec-cis-2-enoyl CoA, oct-cis-2-enoyl CoA and oct-trans-2-enoyl CoA as substrates with Km values of 2.5×10-6M, 1.1×10-6M and 5.0×10-7M, respectively, while another fraction (Type-II) having smaller molecular weight utilizes these substrates with Km values of 3.0×10-6M, 5.3×10-5M and 1.0×10-5M, respectively. This indicates that there exist comparable differences between these two in their affinities especially for the latter two substrates. Some characterizations, such as, effects of pH and of heat treatment on the activities of these reductase preparations were also investigated.
