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@ARTICLE{Yang:92151,
author = {Yang, L. and Hill, M. and Wang, M. and Panjikar, S. and
Stöckigt, J. and DESY},
title = {{S}tructural basis and enzymatic mechanism of the
biosynthesis of {C}9- from {C}10-monoterpenoid indole
alkaloids},
journal = {Angewandte Chemie / International edition},
volume = {48},
issn = {1433-7851},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {PHPPUBDB-12661},
pages = {5211},
year = {2009},
abstract = {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.},
keywords = {Amino Acid Substitution / Biocatalysis / Carboxylic Ester
Hydrolases: metabolism / Mutant Proteins: metabolism /
Protein Structure, Tertiary / Secologanin Tryptamine
Alkaloids: chemistry / Secologanin Tryptamine Alkaloids:
metabolism / Substrate Specificity / Mutant Proteins (NLM
Chemicals) / Secologanin Tryptamine Alkaloids (NLM
Chemicals) / Carboxylic Ester Hydrolases (NLM Chemicals) /
polyneuridine aldehyde esterase (NLM Chemicals)},
cin = {EMBL},
ddc = {540},
cid = {$I:(DE-H253)EMBL_-2012_-20130307$},
pnm = {FS Beamline without reference (POF1-550)},
pid = {G:(DE-H253)POF1-No-Ref-20130405},
experiment = {EXP:(DE-H253)Unknown-BL-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19496101},
UT = {WOS:000267809800029},
doi = {10.1002/anie.200900150},
url = {https://bib-pubdb1.desy.de/record/92151},
}