Effect of mutations at Met-88 and Met-90 on the biotination of Lys-89 of the apo 1.3S subunit of transcarboxylase.

@article{Shenoy1988EffectOM,
  title={Effect of mutations at Met-88 and Met-90 on the biotination of Lys-89 of the apo 1.3S subunit of transcarboxylase.},
  author={B. C. Shenoy and Sulabha Paranjape and V. L. Murtif and Ganesh K. Kumar and David Samols and Harland G. Wood},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={1988},
  volume={2 9},
  pages={
          2505-11
        }
}
The apo 1.3S subunit of transcarboxylase contains the sequence Ala-87-Met-88-Lys-89-Met-90, and it is Lys-89 that is biotinated. This sequence is highly conserved in all the biotin enzymes that have been sequenced (with the exception of acetyl-CoA carboxylase from chicken liver, which has Val in place of Ala). The role of Met-88 and Met-90 in specifying Lys-89 for biotination by synthetase was examined by site-directed mutagenesis. Genes of the 1.3S subunit coding for Thr-88, Leu-88, or Leu-90… CONTINUE READING