The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. V. Purification and properties of 3-deoxy-D-manno-octulosonate aldolase.
نویسندگان
چکیده
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 -2 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 4C-labeled 3-deoxy-D-manno' octulosonate.
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 241 13 شماره
صفحات -
تاریخ انتشار 1966