• Chemistry, Medicine
• Published in
  Archives of biochemistry and…
  2004
• DOI:10.1016/j.abb.2004.03.016

Identification of Val117 and Arg372 as critical amino acid residues for the activity difference between human CYP2A6 and CYP2A13 in coumarin 7-hydroxylation.

@article{He2004IdentificationOV,
  title={Identification of Val117 and Arg372 as critical amino acid residues for the activity difference between human CYP2A6 and CYP2A13 in coumarin 7-hydroxylation.},
  author={Xiao-Yang He and Jian Li Shen and Wen-Yu Hu and Xinxin Ding and A. Y. Lu and Jun-yan Hong},
  journal={Archives of biochemistry and biophysics},
  year={2004},
  volume={427 2},
  pages={
          143-53
        }
}

• Xiao-Yang He, Jian Li Shen, +3 authors Jun-yan Hong

Human cytochrome P450 (CYP) 2A6 and 2A13 play an important role in catalyzing the metabolism of many environmental chemicals including coumarin, nicotine, and several tobacco-specific carcinogens. Both CYP2A6 and CYP2A13 proteins are composed of 494 amino acid residues. Although CYP2A13 shares a 93.5% identity with CYP2A6 in the amino acid sequence, it is only about one-tenth as active as CYP2A6 in catalyzing coumarin 7-hydroxylation. To identify the key amino acid residues that account for… CONTINUE READING

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