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000092151 1001_ $$aYang, L.
000092151 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000092151 245__ $$aStructural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids
000092151 260__ $$aWeinheim$$bWiley-VCH$$c2009
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000092151 440_0 $$0PERI:(DE-600)2011836-3$$aAngew. Chem. [Engl]$$v48$$x1433-7851
000092151 500__ $$3Converted on 2013-05-30 14:24
000092151 500__ $$3Converted on 2013-06-21 19:21
000092151 520__ $$aCutting 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.
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000092151 650_7 $$00$$2NLM Chemicals$$aMutant Proteins
000092151 650_7 $$00$$2NLM Chemicals$$aSecologanin Tryptamine Alkaloids
000092151 650_7 $$0EC 3.1.1.-$$2NLM Chemicals$$aCarboxylic Ester Hydrolases
000092151 650_7 $$0EC 3.1.1.-$$2NLM Chemicals$$apolyneuridine aldehyde esterase
000092151 650_2 $$2MeSH$$aAmino Acid Substitution
000092151 650_2 $$2MeSH$$aBiocatalysis
000092151 650_2 $$2MeSH$$aCarboxylic Ester Hydrolases: metabolism
000092151 650_2 $$2MeSH$$aMutant Proteins: metabolism
000092151 650_2 $$2MeSH$$aProtein Structure, Tertiary
000092151 650_2 $$2MeSH$$aSecologanin Tryptamine Alkaloids: chemistry
000092151 650_2 $$2MeSH$$aSecologanin Tryptamine Alkaloids: metabolism
000092151 650_2 $$2MeSH$$aSubstrate Specificity
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000092151 7001_ $$aHill, M.
000092151 7001_ $$aWang, M.
000092151 7001_ $$aPanjikar, S.
000092151 7001_ $$aStöckigt, J.
000092151 773__ $$0PERI:(DE-600)2011836-3$$a10.1002/anie.200900150$$gVol. 48, p. 5211$$p5211$$q48<5211$$tAngewandte Chemie / International edition$$v48$$x1433-7851$$y2009
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000092151 9141_ $$a(c) Wiley Interscience.$$y2009
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