2wfm
From Proteopedia
Crystal structure of polyneuridine aldehyde esterase mutant (H244A)
Structural highlights
FunctionPNAE_RAUSE Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmaline.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCutting 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. 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 Angew Chem Int Ed Engl. 2009;48(28):5211-3. PMID:19496101[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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