EC Number   |
Natural Substrates |
|---|
   1.5.1.11 | L-arginine + pyruvate + NADH + H+ |
- |
| 1.5.1.11 | more |
- |
| 1.5.1.11 | more |
the major role of the brain enzyme may be the oxidation of octopine |
| 1.5.1.11 | more |
the enzyme may synthesize lysopine, octopinic acid, and the corresponding Nalpha-derivatives of glutamine |
| 1.5.1.11 | more |
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 |
| 1.5.1.11 | more |
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 |
| 1.5.1.11 | more |
mantle muscle enzyme appears geared for the rapid synthesis of octopine under conditions of muscular work |
| 1.5.1.11 | more |
major physiological role in glycolytic energy poduction during burst swimming |
| 1.5.1.11 | more |
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 |
| 1.5.1.11 | N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O |
- |
