%0 Journal Article
%A Smits, S.H.J.
%A Meyer, T.
%A Müller, A.
%A van Os, N.
%A Stoldt, M.
%A Willbold, D.
%A Schmitt, L.
%A Grieshaber, M.K.
%T Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography
%J PLoS one
%V 5
%@ 1932-6203
%C Lawrence, Kan.
%I PLoS
%M PreJuSER-11495
%P e12312
%D 2010
%Z 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.
%X 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.
%K Agmatine: pharmacology
%K Amino Acid Oxidoreductases: antagonists & inhibitors
%K Amino Acid Oxidoreductases: chemistry
%K Amino Acid Oxidoreductases: metabolism
%K Animals
%K Crystallography, X-Ray
%K Ligands
%K Models, Molecular
%K Nuclear Magnetic Resonance, Biomolecular
%K Pecten: enzymology
%K Protein Binding
%K Protein Structure, Tertiary
%K Ligands (NLM Chemicals)
%K Agmatine (NLM Chemicals)
%K Amino Acid Oxidoreductases (NLM Chemicals)
%K D-octopine dehydrogenase (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:20808820
%2 pmc:PMC2924402
%U <Go to ISI:>//WOS:000281075500029
%R 10.1371/journal.pone.0012312
%U https://juser.fz-juelich.de/record/11495