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Exploring a Unique Class II Diterpene Cyclase: The Modified Catalytic Acid Motif Contributes to Ring Contraction in
Kristin Helwig1, Jun Xie2, Cody Lemke1
1Roy J. Carver Department of Biochemistry, Biophysics & Molecular Biology, Iowa State University, Ames, Iowa 50011, United States.
Abstract:
The class II diterpene cyclase from pleuromutilin biosynthesis contains a unique variant of the otherwise highly conserved DxDD motif (DxDM), which cooperatively serves as the catalytic acid, and uniquely produces an "A" ring contracted product, mutildienyl pyrophosphate (MPP). The correlation between these features was investigated here via substitution of aspartate for methionine, which largely blocks the production of MPP and leads to a novel hydroxylated product, syn-halima-13E-en-5β-ol-15-PP, providing insight into this unique reaction.
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