Bacterial production and purification of phosphorylatable phosphoenolpyruvate carboxylase from tobacco

Biosci Biotechnol Biochem. 1996 Dec;60(12):2089-91. doi: 10.1271/bbb.60.2089.

Abstract

Tobacco phosphoenolpyruvate carboxylase (PEPC) [EC 4.1.1.31] cDNA was efficiently expressed in E. coli under the control of the lacZ promoter. The enzyme, purified to homogeneity, had the same catalytic activity, and was phosphorylated in vitro by maize PEPC kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Lac Operon
  • Nicotiana / enzymology*
  • Phosphoenolpyruvate Carboxylase / biosynthesis*
  • Phosphoenolpyruvate Carboxylase / genetics
  • Phosphoenolpyruvate Carboxylase / isolation & purification
  • Phosphorylation
  • Plants, Toxic*
  • Plasmids
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification

Substances

  • Recombinant Proteins
  • Phosphoenolpyruvate Carboxylase