3C7C

A structural basis for substrate and stereo selectivity in octopine dehydrogenase (ODH-NADH-L-Arginine)

Summary for 3C7C

• Entry DOI: 10.2210/pdb3c7c/pdb
• Related: 3C7A 3C7D
• Descriptor: Octopine dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ARGININE (3 entities in total)
• Functional Keywords: (d, l) stereospecific opine dehydrogenase, oxidoreductase
• Biological source: Pecten maximus (King scallop)
• Total number of polymer chains: 1
• Total formula weight: 44896.01

Authors

Smits, S.H.J.,Mueller, A.,Schmitt, L.,Grieshaber, M.K. (deposition date: 2008-02-07, release date: 2008-07-22, Last modification date: 2024-02-21)

Primary citation

Smits, S.H.,Mueller, A.,Schmitt, L.,Grieshaber, M.K.
A structural basis for substrate selectivity and stereoselectivity in octopine dehydrogenase from Pecten maximus.
J.Mol.Biol., 381:200-211, 2008

PubMed 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.

PubMed: 18599075
DOI: 10.1016/j.jmb.2008.06.003

Experimental method

X-RAY DIFFRACTION (3.1 Å)