PMID:6355062
| Citation |
Donovan, WP and Kushner, SR (1983) Purification and characterization of orotidine-5'-phosphate decarboxylase from Escherichia coli K-12. J. Bacteriol. 156:620-4 |
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| Abstract |
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. |
| Links | |
| Keywords |
Carboxy-Lyases/isolation & purification; Chromatography, Affinity; Drug Stability; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kinetics; Orotidine-5'-Phosphate Decarboxylase/isolation & purification; Orotidine-5'-Phosphate Decarboxylase/metabolism |
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