Purification and properties of 4-hydroxy-2-ketopimelate aldolase from Acinetobacter.
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 Mg(2+) and Mn(2+) ions.
D000150:Acinetobacter / Q000201:enzymology* / Q000378:metabolism; D000421:Alcaligenes / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D000645:Ammonium Sulfate; D002458:Cell Fractionation; D002474:Cell-Free System; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D006358:Hot Temperature; D007783:Lactones / Q000378:metabolism; D008970:Molecular Weight
D000596:Amino Acids; D007783:Lactones; D005634:Fructose-Bisphosphate Aldolase; D000645:Ammonium Sulfate