Identification of unique amino acids that modulate CYP4A7 activity.

@article{Loughran2000IdentificationOU,
  title={Identification of unique amino acids that modulate CYP4A7 activity.},
  author={P A Loughran and Linda J. Roman and Alastair Aitken and R. T. Miller and Bettie Sue Siler Masters},
  journal={Biochemistry},
  year={2000},
  volume={39 49},
  pages={
          15110-20
        }
}
A multifamily sequence alignment of the rabbit CYP4A members with the known structure of CYP102 indicates amino acid differences falling within the so-called substrate recognition site(s) (SRS). Chimeric proteins constructed between CYP4A4 and CYP4A7 indicate that laurate activity is affected by the residues within SRS1 and prostaglandin activity is influenced by SRS2-3. Site-directed mutant proteins of CYP4A7 found laurate and arachidonate activity markedly diminished in the R90W mutant (SRS1… Expand
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