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Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo a pyrene-(7R,8S)-diol- (9S,10R)-epoxide

  1. Author:
    Gu, Y. J.
    Xiao, B.
    Wargo, H. L.
    Bucher, M. H.
    Singh, S. V.
    Ji, X. H.

  2. Author Address

    NCI, Ctr Macromol Crystallog, Frederick, MD 21702 USA NCI, Ctr Macromol Crystallog, Frederick, MD 21702 USA Univ Pittsburgh, Dept Pharmacol, Pittsburgh, PA 15261 USA Univ Pittsburgh, Inst Canc, Pittsburgh, PA 15261 USA Ji XH NCI, Ctr Macromol Crystallog, Frederick, MD 21702 USA
    1. Year: 2003
  2. Journal: Biochemistry
    1. 42
    2. 4
    3. Pages: 917-921
  4. Type of Article: Article
  1. Abstract:

    Murine class alpha glutathione S-transferase subunit types A2 (mGSTA2-2) and A1 (mGSTA1-1) have high catalytic efficiency for glutathione (GSH) conjugation of the ultimate carcinogenic metabolite of benzo[a]pyrene, (+)-anti-7,8-dihydroxy-9,10-oxy- 7,8,9,10-tetrahydrobenzo[a]pyrene, [(+)-anti-BPDE]. Only 10 residues differ between the sequences of mGSTA1-1 and 2-2. However, the catalytic efficiency of mGSTA1-1 for GSH conjugation of (+)-anti-BPDE is >3-fold higher as compared with mGSTA2-2. The crystal structure of mGSTA1-1 in complex with the GSH conjugate of (+)-anti-7,8-dihydroxy9,10-oxy-7,8,9,10- tetrahydrobenzo[a]pyrene (GSBpd) reveals that R216 and 1221 in the last helix play important roles in catalysis [Gu, Y., Singh, S. V., and Ji, X. (2000) Biochemistry 39, 12552-12557]. The crystal structure of mGSTA2-2 in complex with GSBpd has been determined, which reveals a different binding mode of GSBpd. Comparison of the two structures suggests that residues 207 and 221 are responsible for the different binding mode of GSBpd and therefore contribute to the distinct catalytic efficiency of the two isozymes.

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