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Purification and Properties of 4-Hydroxy-2-Ketopimelate Aldolase from Acinetobacter

¹ Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul, Minnesota 55101

ABSTRACT

The chemical synthesis of 4-hydroxy-2-ketopimelic acid is described. An aldolase that cleaves this compound to succinic semialdehyde and pyruvate has been purified from Acinetobacter grown at the expense of 4-hydroxyphenylacetic acid. The molecular weight of the enzyme was about 158,000 from sedimentation equilibrium data; other physical determinations gave values in reasonable agreement. The protein was globular and was dissociated in sodium dodecyl sulfate to give a species of molecular weight 25,700. The enzyme attacked both enantiomers of synthetic 4-hydroxy-2-ketopimelate and was stimulated by Mg²⁺ and Mn²⁺ ions.