Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein.

@article{Campeau2001ExpressionIE,
  title={Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein.},
  author={E Campeau and R. A. Gravel},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 15},
  pages={12310-6}
}
Biotin functions as a covalently bound cofactor of biotindependent carboxylases. Biotin attachment is catalyzed by biotin protein ligases, called holocarboxylase synthetase in mammals and BirA in prokaryotes. These enzymes show a high degree of sequence similarity in their biotinylation domains but differ markedly in the length and sequence of their N terminus. BirA is also the repressor of the biotin operon, and its DNA attachment site is located in its N terminus. The function of the… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

Similar Papers

Loading similar papers…