The Biosynthesis of Cell Wall Lipopolysaccharide in Escherichia coli

V. PURIFICATION AND PROPERTIES OF 3-DEOXY-D-MANNO-OCTULOSONATE ALDOLASE

From the ¹ From the Rackham Arthritis Research Unit and Department of Microbiology, The University of Michigan, Ann Arbor, Michigan, and the Department of Physiological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

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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