Revised structure of aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Evidence for four identical subunits.

@article{FalcozKelly1972RevisedSO,
  title={Revised structure of aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Evidence for four identical subunits.},
  author={Francoise Falcoz-Kelly and J. P. Janin and John C. Saari and Michel V{\'e}ron and P Truffa-bachi and G. N. Cohen},
  journal={European journal of biochemistry},
  year={1972},
  volume={28 4},
  pages={
          507-19
        }
}
After revision, the molecular weight of the subunit of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I is 86000 ± 4000 instead of 60000 as previously published. The enzyme is a tetramer, not an hexamer. The electrophoretic homogeneity of the subunits, the number of unique sequences around cysteinyl and tryptophanyl residues, the determination of the N-terminal and C-terminal sequences all point to the probable identity of the four subunits. After revision of the molecular… CONTINUE READING