Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography
| Autor: | Sander H. J. Smits, Tatu Meyer, Nadine van Os, Lutz Schmitt, Andre Mueller, Manfred K. Grieshaber, Dieter Willbold, Matthias Stoldt |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Agmatine Stereochemistry Science Biophysics Dehydrogenase Plasma protein binding Crystallography X-Ray Ligands Biochemistry antagonists & inhibitors [Amino Acid Oxidoreductases] chemistry.chemical_compound Oxidoreductase Animals Pecten maximus Nuclear Magnetic Resonance Biomolecular pharmacology [Agmatine] Biochemistry/Experimental Biophysical Methods chemistry.chemical_classification Octopine Pecten Multidisciplinary biology Nuclear magnetic resonance spectroscopy biology.organism_classification Protein Structure Tertiary D-octopine dehydrogenase metabolism [Amino Acid Oxidoreductases] enzymology [Pecten] chemistry Medicine ddc:500 chemistry [Amino Acid Oxidoreductases] Amino Acid Oxidoreductases NAD+ kinase Research Article Protein Binding |
| Zdroj: | PLoS ONE, Vol 5, Iss 8, p e12312 (2010) PLoS ONE PLoS one 5, e12312 (2010). doi:10.1371/journal.pone.0012312 |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0012312 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|