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Publication Detail

Title: Dihydroorotase from Escherichia coli. Cloning the pyrC gene and production of tryptic peptide maps.

Authors: Brown, D C; Collins, K D

Published In J Biol Chem, (1986 May 05)

Abstract: We have inserted a 1.7-kilobase pair Escherichia coli DNA fragment containing the 1-kilobase pair pyrC gene into the high copy number plasmid pKC16. Dihydroorotase expressed by the pyrC plasmid in E. coli constituted 6.3% of the soluble protein in frozen cell paste. Pure dihydroorotase derived from this frozen cell paste was compared with pure enzyme derived from an E. coli strain lacking the pyrC plasmid: tryptic peptide maps from the two dihydroorotase preparations, produced using reverse-phase high performance liquid chromatography, were indistinguishable. We conclude that the entire pyrC gene is present on the hybrid plasmid and that the dihydroorotase produced from this plasmid is identical to the wild type.

PubMed ID: 2871019 Exiting the NIEHS site

MeSH Terms: Amidohydrolases/genetics*; Cloning, Molecular*; DNA Restriction Enzymes; Dihydroorotase/genetics*; Escherichia coli/enzymology*; Escherichia coli/genetics; Genes*; Genes, Bacterial*; Kinetics; Peptide Fragments/analysis; Plasmids; Trypsin

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