Identification of Amino Acid Residues Essential for Onion Lachrymatory Factor Synthase Activity

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Abstract

Lachrymatory factor synthase (LFS), an enzyme essential for the synthesis of the onion lachrymatory factor (propanethial <I>S</I>-oxide), was identified in 2002. This was the first reported enzyme involved in the production of thioaldehyde <I>S</I>-oxides <I>via</I> an intra-molecular H<SUP>+</SUP> substitution reaction, and we therefore attempted to identify the catalytic amino acid residues of LFS as the first step in elucidating the unique catalytic reaction mechanism of this enzyme. A comparison of the LFS cDNA sequences among lachrymatory <I>Allium</I> plants, a deletion analysis and site-directed mutagenesis enabled us to identify two amino acids (Arg71 and Glu88) that were indispensable to the LFS activity. Homology modeling was performed for LFS/23–169 on the basis of the template structure of a pyrabactin resistance 1-like protein (PYL) which had been selected from a BLASTP search on SWISS-MODEL against LFS/23–169. We identified in the modeled structure of LFS a pocket corresponding to the ligand-binding site in PYL, and Arg71 and Glu88 were located in this pocket.

Journal

  • Bioscience, Biotechnology, and Biochemistry

    Bioscience, Biotechnology, and Biochemistry 76(3), 447-453, 2012-03-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

References:  31

Codes

  • NII Article ID (NAID)
    10030750283
  • NII NACSIS-CAT ID (NCID)
    AA10824164
  • Text Lang
    ENG
  • Article Type
    ART
  • ISSN
    09168451
  • NDL Article ID
    023553661
  • NDL Call No.
    Z53-G223
  • Data Source
    CJP  NDL  J-STAGE 
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