Yang, L., Hill, M., Wang, M., Panjikar, S., Stoeckigt, J.
Ligand
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Reference
Title: Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids Yang L, Hill M, Wang M, Panjikar S, Stockigt J Ref: Angew Chem Int Ed Engl, 48:5211, 2009 : PubMed
Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.
Representative scheme of Hydroxynitrile_lyase structure and an image from PDBsum server
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2WFLFold classification based on Structure-Structure alignment of Proteins - FSSP server
