Journal Article

PHPPUBDB-12661

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids

Yang, L. ; Hill, M. ; Wang, M. ; Panjikar, S. ; Stöckigt, J. ; DESY

2009
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/anie.200900150

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.

Keyword(s): Amino Acid Substitution (MeSH) ; Biocatalysis (MeSH) ; Carboxylic Ester Hydrolases: metabolism (MeSH) ; Mutant Proteins: metabolism (MeSH) ; Protein Structure, Tertiary (MeSH) ; Secologanin Tryptamine Alkaloids: chemistry (MeSH) ; Secologanin Tryptamine Alkaloids: metabolism (MeSH) ; Substrate Specificity (MeSH) ; Mutant Proteins ; Secologanin Tryptamine Alkaloids ; Carboxylic Ester Hydrolases ; polyneuridine aldehyde esterase

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Contributing Institute(s):

1. European Molecular Biology Laboratory (EMBL)

Research Program(s):

1. FS Beamline without reference (POF1-550) (POF1-550)

Experiment(s):

1. Unknown DESY Beamline

Appears in the scientific report 2009
Notes: (c) Wiley Interscience.

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Database coverage:
; ; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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