Site-directed mutagenesis of phosphorylation sites of the branched chain alpha-ketoacid dehydrogenase complex.

@article{Zhao1994SitedirectedMO,
  title={Site-directed mutagenesis of phosphorylation sites of the branched chain alpha-ketoacid dehydrogenase complex.},
  author={Yinzhi Zhao and John W. Hawes and Kirill M Popov and Jerzy Jaskiewicz and Yoshiharu Shimomura and David W Crabb and Robert A. Harris},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 28},
  pages={18583-7}
}
Regulation of the branched chain alpha-ketoacid dehydrogenase complex, the rate-limiting enzyme of branched chain amino acid catabolism, involves phosphorylation of 2 amino acid residues (site 1, serine 293; site 2, serine 303). To directly assess the roles played by these sites, site-directed mutagenesis was used to convert these serines to glutamates and/or alanines. Functional E1 heterotetramers were expressed in Escherichia coli carrying genes for E1 alpha and E1 beta under control of… CONTINUE READING

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