TY  - JOUR
AU  - Yang, L.
AU  - Hill, M.
AU  - Wang, M.
AU  - Panjikar, S.
AU  - Stöckigt, J.
AU  - DESY
TI  - Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids
JO  - Angewandte Chemie / International edition
VL  - 48
SN  - 1433-7851
CY  - Weinheim
PB  - Wiley-VCH
M1  - PHPPUBDB-12661
SP  - 5211
PY  - 2009
AB  - 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.
KW  - Amino Acid Substitution
KW  - Biocatalysis
KW  - Carboxylic Ester Hydrolases: metabolism
KW  - Mutant Proteins: metabolism
KW  - Protein Structure, Tertiary
KW  - Secologanin Tryptamine Alkaloids: chemistry
KW  - Secologanin Tryptamine Alkaloids: metabolism
KW  - Substrate Specificity
KW  - Mutant Proteins (NLM Chemicals)
KW  - Secologanin Tryptamine Alkaloids (NLM Chemicals)
KW  - Carboxylic Ester Hydrolases (NLM Chemicals)
KW  - polyneuridine aldehyde esterase (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:19496101
UR  - <Go to ISI:>//WOS:000267809800029
DO  - DOI:10.1002/anie.200900150
UR  - https://bib-pubdb1.desy.de/record/92151
ER  -