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000011495 0247_ $$2DOI$$a10.1371/journal.pone.0012312
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000011495 084__ $$2WoS$$aBiology
000011495 1001_ $$0P:(DE-Juel1)VDB94800$$aSmits, S.H.J.$$b0$$uFZJ
000011495 245__ $$aInsights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography
000011495 260__ $$aLawrence, Kan.$$bPLoS$$c2010
000011495 300__ $$ae12312
000011495 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000011495 440_0 $$018181$$aPLOS One$$v19$$x1932-6203$$y8
000011495 500__ $$aThis 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.
000011495 520__ $$aOctopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to octopine, NAD(+), and water during escape swimming and/or subsequent recovery. The structure of OcDH was recently solved and a reaction mechanism was proposed which implied an ordered binding of NADH, L-arginine and finally pyruvate. Here, the order of substrate binding as well as the underlying conformational changes were investigated by NMR confirming the model derived from the crystal structures. Furthermore, the crystal structure of the OcDH/NADH/agmatine complex was determined which suggests a key role of the side chain of L-arginine in protein cataylsis. Thus, the order of substrate binding to OcDH as well as the molecular signals involved in octopine formation can now be described in molecular detail.
000011495 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000011495 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000011495 588__ $$aDataset connected to Web of Science, Pubmed
000011495 650_2 $$2MeSH$$aAgmatine: pharmacology
000011495 650_2 $$2MeSH$$aAmino Acid Oxidoreductases: antagonists & inhibitors
000011495 650_2 $$2MeSH$$aAmino Acid Oxidoreductases: chemistry
000011495 650_2 $$2MeSH$$aAmino Acid Oxidoreductases: metabolism
000011495 650_2 $$2MeSH$$aAnimals
000011495 650_2 $$2MeSH$$aCrystallography, X-Ray
000011495 650_2 $$2MeSH$$aLigands
000011495 650_2 $$2MeSH$$aModels, Molecular
000011495 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000011495 650_2 $$2MeSH$$aPecten: enzymology
000011495 650_2 $$2MeSH$$aProtein Binding
000011495 650_2 $$2MeSH$$aProtein Structure, Tertiary
000011495 650_7 $$00$$2NLM Chemicals$$aLigands
000011495 650_7 $$0306-60-5$$2NLM Chemicals$$aAgmatine
000011495 650_7 $$0EC 1.4.-$$2NLM Chemicals$$aAmino Acid Oxidoreductases
000011495 650_7 $$0EC 1.5.1.11$$2NLM Chemicals$$aD-octopine dehydrogenase
000011495 650_7 $$2WoSType$$aJ
000011495 7001_ $$0P:(DE-Juel1)VDB7071$$aMeyer, T.$$b1$$uFZJ
000011495 7001_ $$0P:(DE-Juel1)VDB1103$$aMüller, A.$$b2$$uFZJ
000011495 7001_ $$0P:(DE-Juel1)VDB94801$$avan Os, N.$$b3$$uFZJ
000011495 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b4$$uFZJ
000011495 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b5$$uFZJ
000011495 7001_ $$0P:(DE-Juel1)VDB29801$$aSchmitt, L.$$b6$$uFZJ
000011495 7001_ $$0P:(DE-Juel1)VDB94802$$aGrieshaber, M.K.$$b7$$uFZJ
000011495 773__ $$0PERI:(DE-600)2267670-3$$a10.1371/journal.pone.0012312$$gVol. 5, p. e12312$$pe12312$$q5<e12312$$tPLoS one$$v5$$x1932-6203$$y2010
000011495 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924402
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