Literature summary for 1.5.1.11 extracted from

Smits, S.H.; Meyer, T.; Mueller, A.; van Os, N.; Stoldt, M.; Willbold, D.; Schmitt, L.; Grieshaber, M.K.
Insights into the mechanism of ligand binding to octopine dehydrogenase from Pecten maximus by NMR and crystallography (2010), PLoS ONE, 5, e12312.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with NADH and agmatine, to 2.8 A resolution	Pecten maximus

Organism

Organism	UniProt	Comment	Textmining
Pecten maximus	Q9BHM6	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+	substrates bind in an ordered sequential manner. First NADH binds to OcDH followed by L-arginine. The binding of the guanidinium headgroup of L-arginine induces a conformational change, resulting in the formation of the pyruvate binding site. The reduction of pyruvate can only occur in the presence of L-arginine, which than forms octopine and prevents lactate formation	Pecten maximus	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	adductor muscle	Pecten maximus	-

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Release 2023.1 (January 2023)