Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.

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...

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Autores principales:	Sander H J Smits, Tatu Meyer, Andre Mueller, Nadine van Os, Matthias Stoldt, Dieter Willbold, Lutz Schmitt, Manfred K Grieshaber
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e6a886ffa13c42bfbacf17dedcbdb213
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spelling	oai:doaj.org-article:e6a886ffa13c42bfbacf17dedcbdb2132021-11-18T06:35:54ZInsights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.1932-620310.1371/journal.pone.0012312https://doaj.org/article/e6a886ffa13c42bfbacf17dedcbdb2132010-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20808820/?tool=EBIhttps://doaj.org/toc/1932-6203Octopine 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.Sander H J SmitsTatu MeyerAndre MuellerNadine van OsMatthias StoldtDieter WillboldLutz SchmittManfred K GrieshaberPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 8, p e12312 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sander H J Smits Tatu Meyer Andre Mueller Nadine van Os Matthias Stoldt Dieter Willbold Lutz Schmitt Manfred K Grieshaber Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.
description	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.
format	article
author	Sander H J Smits Tatu Meyer Andre Mueller Nadine van Os Matthias Stoldt Dieter Willbold Lutz Schmitt Manfred K Grieshaber
author_facet	Sander H J Smits Tatu Meyer Andre Mueller Nadine van Os Matthias Stoldt Dieter Willbold Lutz Schmitt Manfred K Grieshaber
author_sort	Sander H J Smits
title	Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.
title_short	Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.
title_full	Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.
title_fullStr	Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.
title_full_unstemmed	Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.
title_sort	insights into the mechanism of ligand binding to octopine dehydrogenase from pecten maximus by nmr and crystallography.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/e6a886ffa13c42bfbacf17dedcbdb213
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Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography.

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