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| Home > Publications database > Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids > print |
| 001 | 92151 | ||
| 005 | 20250718144127.0 | ||
| 024 | 7 | _ | |a pmid:19496101 |2 pmid |
| 024 | 7 | _ | |a 0570-0833 |2 ISSN |
| 024 | 7 | _ | |a 1433-7851 |2 ISSN |
| 024 | 7 | _ | |a 1521-3773 |2 ISSN |
| 024 | 7 | _ | |a 0044-8249 |2 ISSN |
| 024 | 7 | _ | |a 10.1002/anie.200900150 |2 doi |
| 024 | 7 | _ | |a WOS:000267809800029 |2 WOS |
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| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Yang, L. |
| 110 | 1 | _ | |a DESY |b European Molecular Biology Laboratory |
| 245 | _ | _ | |a Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids |
| 260 | _ | _ | |a Weinheim |c 2009 |b Wiley-VCH |
| 300 | _ | _ | |a 5211 |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 440 | _ | 0 | |a Angew. Chem. [Engl] |0 PERI:(DE-600)2011836-3 |v 48 |x 1433-7851 |
| 500 | _ | _ | |3 Converted on 2013-05-30 14:24 |
| 500 | _ | _ | |3 Converted on 2013-06-21 19:21 |
| 520 | _ | _ | |a 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. |
| 536 | _ | _ | |0 G:(DE-H253)POF1-No-Ref-20130405 |f POF I |x 0 |c POF1-550 |a FS Beamline without reference (POF1-550) |
| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 7 | |a Mutant Proteins |0 0 |2 NLM Chemicals |
| 650 | _ | 7 | |a Secologanin Tryptamine Alkaloids |0 0 |2 NLM Chemicals |
| 650 | _ | 7 | |a Carboxylic Ester Hydrolases |0 EC 3.1.1.- |2 NLM Chemicals |
| 650 | _ | 7 | |a polyneuridine aldehyde esterase |0 EC 3.1.1.- |2 NLM Chemicals |
| 650 | _ | 2 | |a Amino Acid Substitution |2 MeSH |
| 650 | _ | 2 | |a Biocatalysis |2 MeSH |
| 650 | _ | 2 | |a Carboxylic Ester Hydrolases: metabolism |2 MeSH |
| 650 | _ | 2 | |a Mutant Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Structure, Tertiary |2 MeSH |
| 650 | _ | 2 | |a Secologanin Tryptamine Alkaloids: chemistry |2 MeSH |
| 650 | _ | 2 | |a Secologanin Tryptamine Alkaloids: metabolism |2 MeSH |
| 650 | _ | 2 | |a Substrate Specificity |2 MeSH |
| 693 | _ | _ | |0 EXP:(DE-H253)Unknown-BL-20150101 |f Unknown DESY Beamline |x 0 |6 EXP:(DE-H253)Unknown-BL-20150101 |
| 700 | 1 | _ | |a Hill, M. |
| 700 | 1 | _ | |a Wang, M. |
| 700 | 1 | _ | |a Panjikar, S. |
| 700 | 1 | _ | |a Stöckigt, J. |
| 773 | _ | _ | |a 10.1002/anie.200900150 |g Vol. 48, p. 5211 |0 PERI:(DE-600)2011836-3 |q 48<5211 |p 5211 |t Angewandte Chemie / International edition |v 48 |y 2009 |x 1433-7851 |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/92151/files/manuscript.doc |y OpenAccess |
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| 914 | 1 | _ | |a (c) Wiley Interscience. |y 2009 |
| 915 | _ | _ | |a JCR/ISI refereed |0 StatID:(DE-HGF)0010 |2 StatID |
| 915 | _ | _ | |a Peer review |0 StatID:(DE-HGF)0030 |2 StatID |
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| 915 | _ | _ | |a No Author Disambiguation |0 StatID:(DE-HGF)1 |2 StatID |
| 920 | _ | 1 | |i Experiments with synchrotron radiation |k HASYLAB |
| 920 | 1 | _ | |0 I:(DE-H253)EMBL_-2012_-20130307 |k EMBL |l European Molecular Biology Laboratory |x 0 |
| 920 | _ | _ | |k 001 |
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