Abstract
Abstract 3-Deoxy-D-manno-octulosonate aldolase, an inducible enzyme isolated from extracts of 3-deoxy-D-manno-octulosonate-grown Aerobacter cloacae, has been purified approximately 60-fold. The enzyme catalyzes the following reaction: 3-deoxy-D-manno-octulosonate ⇄ pyruvate + D-arabinose. Pyruvate was characterized chromatographically and with lactic acid dehydrogenase. D-Arabinose was characterized chromatographically and by its reactivity with L-fucose isomerase to form D-ribulose. The purified enzyme exhibited the following properties: pH optimum, 7; Michaelis constant = 6 x 10-3 M; and equilibrium constant = 0.077 M. The enzyme provides a convenient method for the preparation of specifically 14C-labeled 3-deoxy-D-manno-octulosonate.
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