%0 Journal Article
%A Yang, L.
%A Hill, M.
%A Wang, M.
%A Panjikar, S.
%A Stöckigt, J.
%A DESY
%T Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids
%J Angewandte Chemie / International edition
%V 48
%@ 1433-7851
%C Weinheim
%I Wiley-VCH
%M PHPPUBDB-12661
%P 5211
%D 2009
%X 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.
%K Amino Acid Substitution
%K Biocatalysis
%K Carboxylic Ester Hydrolases: metabolism
%K Mutant Proteins: metabolism
%K Protein Structure, Tertiary
%K Secologanin Tryptamine Alkaloids: chemistry
%K Secologanin Tryptamine Alkaloids: metabolism
%K Substrate Specificity
%K Mutant Proteins (NLM Chemicals)
%K Secologanin Tryptamine Alkaloids (NLM Chemicals)
%K Carboxylic Ester Hydrolases (NLM Chemicals)
%K polyneuridine aldehyde esterase (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19496101
%U <Go to ISI:>//WOS:000267809800029
%R 10.1002/anie.200900150
%U https://bib-pubdb1.desy.de/record/92151