Isolation and characterization of a cDNA fromCuphea lanceolata encoding a β-ketoacyl-ACP reductase

@article{Klein1992IsolationAC,
  title={Isolation and characterization of a cDNA fromCuphea lanceolata encoding a β-ketoacyl-ACP reductase},
  author={Barbara Klein and Katharina Pawlowski and Christa H{\"o}ricke-Grandpierre and J. L. Schell and Reinhard T{\"o}pfer},
  journal={Molecular and General Genetics MGG},
  year={1992},
  volume={233},
  pages={122-128}
}
A cDNA encoding β-ketoacyl-ACP reductase (EC 1.1.1.100), an integral part of the fatty acid synthase type II, was cloned fromCuphea lanceolata. This cDNA of 1276 by codes for a polypeptide of 320 amino acids with 63 N-terminal residues presumably representing a transit peptide and 257 residues corresponding to the mature protein of 27 kDa. The encoded… CONTINUE READING