Purification and characterization of orotidine-5'-phosphate decarboxylase from Escherichia coli K-12.
Using blue Sepharose affinity chromatography, we purified orotidine-5'-phosphate decarboxylase over 600-fold, to near homogeneity, from strains of Escherichia coli harboring the cloned pyrF gene on the multicopy plasmid pDK26. The purified enzyme has a subunit molecular weight of 27,000 but appears to be catalytically active as a dimer. In contrast to yeast enzymes, orotidine-5'-phosphate decarboxylase from E. coli is unstable at pH 6.0. The specific activity and Km values were 220 U/mg and 6 microM, respectively.
D002262:Carboxy-Lyases / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D004355:Drug Stability; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000302:isolation & purification* / Q000378:metabolism
D002262:Carboxy-Lyases; D009964:Orotidine-5'-Phosphate Decarboxylase