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A three-dimensional model of renilla luciferase Keith V. Wood*; MG Gruber Promega, 2800 Woods Hollow Rd, Madison, WI 53711, USA      *(kwood@promega.com) Amino acid sequence homology reveals that Renilla luciferase belongs to a broad structural class called a/b hydrolases. Renilla luciferase is most closely related to several haloalkane dehalogenases that form a functional subset within the a/b hydrolase family. The degree of sequence similarity suggests that Renilla luciferase evolved from a haloalkane dehalogenase or a closely related enzyme. It is thus likely that Renilla luciferase also shares a similar catalytic mechanism. Characteristic of the a/b hydrolases, the haloalkane dehalogenases function through the action of a catalytic triad analogous to the serine proteases. This catalytic triad may be the basis for the bioluminescence of Renilla luciferase. A three-dimensional model of Renilla luciferase could also be developed based on the crystal structure solved previously for the haloalkane dehalogenases. [Talk: wood.keithv.95131]

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