Home > Publications database > Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography > print

001     11495
005     20200423202824.0
024 7 _ |a pmid:20808820
|2 pmid
024 7 _ |a pmc:PMC2924402
|2 pmc
024 7 _ |a 10.1371/journal.pone.0012312
|2 DOI
024 7 _ |a WOS:000281075500029
|2 WOS
024 7 _ |a 2128/11184
|2 Handle
037 _ _ |a PreJuSER-11495
041 _ _ |a eng
082 _ _ |a 500
084 _ _ |2 WoS
|a Biology
100 1 _ |0 P:(DE-Juel1)VDB94800
|a Smits, S.H.J.
|b 0
|u FZJ
245 _ _ |a Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography
260 _ _ |a Lawrence, Kan.
|b PLoS
|c 2010
300 _ _ |a e12312
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 18181
|a PLOS One
|v 19
|x 1932-6203
|y 8
500 _ _ |a This work was supported by the Deutsche Forschungs Gemeinschaft (grant GR456/20-4 to M.K.G.) and a stipendium of the North Rhein Westphalia graduate school Biostruct to T.M. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
520 _ _ |a Octopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to octopine, NAD(+), and water during escape swimming and/or subsequent recovery. The structure of OcDH was recently solved and a reaction mechanism was proposed which implied an ordered binding of NADH, L-arginine and finally pyruvate. Here, the order of substrate binding as well as the underlying conformational changes were investigated by NMR confirming the model derived from the crystal structures. Furthermore, the crystal structure of the OcDH/NADH/agmatine complex was determined which suggests a key role of the side chain of L-arginine in protein cataylsis. Thus, the order of substrate binding to OcDH as well as the molecular signals involved in octopine formation can now be described in molecular detail.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
536 _ _ |0 G:(DE-Juel1)FUEK505
|2 G:(DE-HGF)
|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Agmatine: pharmacology
650 _ 2 |2 MeSH
|a Amino Acid Oxidoreductases: antagonists & inhibitors
650 _ 2 |2 MeSH
|a Amino Acid Oxidoreductases: chemistry
650 _ 2 |2 MeSH
|a Amino Acid Oxidoreductases: metabolism
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Ligands
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Pecten: enzymology
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 306-60-5
|2 NLM Chemicals
|a Agmatine
650 _ 7 |0 EC 1.4.-
|2 NLM Chemicals
|a Amino Acid Oxidoreductases
650 _ 7 |0 EC 1.5.1.11
|2 NLM Chemicals
|a D-octopine dehydrogenase
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-Juel1)VDB7071
|a Meyer, T.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB1103
|a Müller, A.
|b 2
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB94801
|a van Os, N.
|b 3
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB21601
|a Stoldt, M.
|b 4
|u FZJ
700 1 _ |0 P:(DE-Juel1)132029
|a Willbold, D.
|b 5
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB29801
|a Schmitt, L.
|b 6
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB94802
|a Grieshaber, M.K.
|b 7
|u FZJ
773 _ _ |0 PERI:(DE-600)2267670-3
|a 10.1371/journal.pone.0012312
|g Vol. 5, p. e12312
|p e12312
|q 5|t PLoS one
|v 5
|x 1932-6203
|y 2010
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924402
856 4 _ |u https://juser.fz-juelich.de/record/11495/files/journal.pone.0012312.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/11495/files/journal.pone.0012312.gif?subformat=icon
|x icon
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/11495/files/journal.pone.0012312.jpg?subformat=icon-180
|x icon-180
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/11495/files/journal.pone.0012312.jpg?subformat=icon-700
|x icon-700
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/11495/files/journal.pone.0012312.pdf?subformat=pdfa
|x pdfa
|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:11495
|p openaire
|p open_access
|p driver
|p VDB
|p dnbdelivery
913 1 _ |0 G:(DE-Juel1)FUEK409
|a DE-HGF
|b Gesundheit
|k P33
|l Funktion und Dysfunktion des Nervensystems
|v Funktion und Dysfunktion des Nervensystems
|x 0
913 1 _ |0 G:(DE-Juel1)FUEK505
|a DE-HGF
|b Schlüsseltechnologien
|k P45
|l Biologische Informationsverarbeitung
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|x 1
914 1 _ |y 2010
915 _ _ |a Creative Commons Attribution CC BY 3.0
|0 LIC:(DE-HGF)CCBY3
|2 HGFVOC
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
|2 StatID
915 _ _ |a JCR/ISI refereed
|0 StatID:(DE-HGF)0010
920 1 _ |0 I:(DE-Juel1)VDB942
|d 31.12.2010
|g ISB
|k ISB-3
|l Strukturbiochemie
|x 0
970 _ _ |a VDB:(DE-Juel1)122657
980 1 _ |a FullTexts
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21