Biotin sulfoxide reductase: Tryptophan 90 is required for efficient substrate utilization.

@article{Pollock2003BiotinSR,
  title={Biotin sulfoxide reductase: Tryptophan 90 is required for efficient substrate utilization.},
  author={Veronica V Pollock and Richard C Conover and Michael K. Johnson and Michael J. Barber},
  journal={Archives of biochemistry and biophysics},
  year={2003},
  volume={409 2},
  pages={315-26}
}
Rhodobacter sphaeroides f. sp. denitrificans biotin sulfoxide reductase (BSOR) catalyzes the reduction of d-biotin d-sulfoxide to biotin and contains the molybdopterin guanine dinucleotide (MGD) cofactor as its sole prosthetic group. Comparison of the primary sequences of BSOR and the closely related enzyme dimethyl sulfoxide reductase (DMSOR) indicated a number of conserved residues, including an active-site tryptophan residue (W90), which has been suggested to be involved in hydrogen bonding… CONTINUE READING