Folding requirements are different between sterol 14alpha-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs.

@article{Lepesheva2001FoldingRA,
  title={Folding requirements are different between sterol 14alpha-demethylase (CYP51) from Mycobacterium tuberculosis and human or fungal orthologs.},
  author={Galina I Lepesheva and Larissa M Podust and Aouatef Bellamine and Michael R. Waterman},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 30},
  pages={28413-20}
}
Upon sequence alignment of CYP51 sterol 14alpha-demethylase from animals, plants, fungi, and bacteria, arginine corresponding to Arg-448 of CYP51 in Mycobacterium tuberculosis (MT) is conserved near the C terminus of all family members. In MTCYP51 Arg-448 forms a salt bridge with Asp-287, connecting beta-strand 3-2 with helix J. Deletion of the three C-terminal residues of MTCYP51 has little effect on expression of P450 in Escherichia coli. However, truncation of the fourth amino acid (Arg-448… CONTINUE READING

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