A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus
In: Journal of Molecular Biology, Jg. 381 (2008-08-01), Heft 1, S. 200-211
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Zugriff:
Abstract: Octopine dehydrogenase [N 2-(d-1-carboxyethyl)-l-arginine:NAD+ oxidoreductase] (OcDH) from the adductor muscle of the great scallop Pecten maximus catalyzes the reductive condensation of l-arginine and pyruvate to octopine during escape swimming. This enzyme, which is a prototype of opine dehydrogenases (OpDHs), oxidizes glycolytically born NADH to NAD+, thus sustaining anaerobic ATP provision during short periods of strenuous muscular activity. In contrast to some other OpDHs, OcDH uses only l-arginine as the amino acid substrate. Here, we report the crystal structures of OcDH in complex with NADH and the binary complexes NADH/l-arginine and NADH/pyruvate, providing detailed information about the principles of substrate recognition, ligand binding and the reaction mechanism. OcDH binds its substrates through a combination of electrostatic forces and size selection, which guarantees that OcDH catalysis proceeds with substrate selectivity and stereoselectivity, giving rise to a second chiral center and exploiting a “molecular ruler” mechanism. [Copyright &y& Elsevier]
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A Structural Basis for Substrate Selectivity and Stereoselectivity in Octopine Dehydrogenase from Pecten maximus
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Autor/in / Beteiligte Person: | Smits, Sander H.J. ; Mueller, Andre ; Schmitt, Lutz ; Grieshaber, Manfred K. |
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Zeitschrift: | Journal of Molecular Biology, Jg. 381 (2008-08-01), Heft 1, S. 200-211 |
Veröffentlichung: | 2008 |
Medientyp: | academicJournal |
ISSN: | 0022-2836 (print) |
DOI: | 10.1016/j.jmb.2008.06.003 |
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