1.5.1.11: D-octopine dehydrogenase
This is an abbreviated version!
For detailed information about D-octopine dehydrogenase, go to the full flat file.
Reaction
Synonyms
D-Octopine synthase, Dehydrogenase, octopine, flavin-containing opine dehydrogenase, N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase, N2-(D-1-carboxyethyl)-L-arginine:NAD+-oxidoreductase, OcDH, OCS, Octopine dehydrogenase, Octopine synthase, Octopine:NAD oxidoreductase, ODH, pTi_008
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Natural Substrates Products
Natural Substrates Products on EC 1.5.1.11 - D-octopine dehydrogenase
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REACTION DIAGRAM
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
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L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
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L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
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r
L-arginine + pyruvate + NADH + H+
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
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L-arginine + pyruvate + NADH + H+
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N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
L-arginine + pyruvate + NADH + H+
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octopine [N2-(1-D-carboxyethyl)-L-arginine] is synthesized by a NAD(P)H-dependent soluble dehydrogenase that catalyzes the reductive condensation of pyruvate with L-arginine. Although the reaction may be reversible in vitro, the frequent use of the term synthase rather than dehydrogenase has emphasized the importance of biosynthesis, but not degradation, and distinguishes it from the mollusk octopine dehydrogenase
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additional information
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the enzyme may synthesize lysopine, octopinic acid, and the corresponding Nalpha-derivatives of glutamine
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additional information
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the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
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additional information
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the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
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additional information
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octopine is produced in the mantle via the reaction of the muscle isoenzyme and is subsequently flushed out into the blood and transported to other tissues such as the optic lobe for re-oxidation via the optic lobe isoenzyme
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additional information
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the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
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additional information
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the major role of the brain enzyme may be the oxidation of octopine
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additional information
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the evolutionary development of the enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrate L-Arg, and pyruvate only. This trend is correlated with an increasing importance of the enzyme in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups
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additional information
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mantle muscle enzyme appears geared for the rapid synthesis of octopine under conditions of muscular work
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additional information
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major physiological role in glycolytic energy poduction during burst swimming
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