Substrate specificities of octopine dehydrogenases from marine invertebrates

Storey, Kenneth B. and Dando, Paul R. 1982 Substrate specificities of octopine dehydrogenases from marine invertebrates. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 73 (3). 521-528. https://doi.org/10.1016/0305-0491(82)90069-4

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Abstract/Summary

1. Amino acid, keto acid and imino acid substrate specificities of octopine dehydrogenase (ODH) from seven marine invertebrate sources were investigated. 2. Three groups of ODH enzymes were identified determined, largely, by their use of L-lysine as an alternative amino acid substrate. 3. The broadly specific ODH from the sea anemone, Calliactes parasitica, utilized L-arginine and L-lysine at equal rates showing a substrate site able to utilize both guanidino and non-guanidino amino acids. Keto acid specificity was also broad; apparent Km's for pyruvate, oxaloacetate and α-ketobutyrate were similar. Both D-octopine and D-lysopine were oxidized by the enzyme. 4. ODH from 3 bivalves, Mytilus edulis, Cerastoderma edule and Glycymeris glycymeris and from the cephalopod, Sepia officinalis showed lower rates of enzyme activity with L-lysine or L-ornithine (3–79% of L-arginine activity), lower rates with alternative guanidino amino acids, L-homoarginine and L-canavanine, and higher apparent Km's for alternative keto acids compared to the sea anemone enzyme. Mantle muscle ODH from S. officinalis, with its major physiological role in glycolytic energy production during burst swimming, showed the highest specificity for l-arginine of all enzymes examined. 5. ODH from the bivalve, Arctica islandica, showed no activity in the presence of non-guanidino amino acids. 6. The evolutionary development of the ODH enzyme appears to have led from a broadly specific imino acid dehydrogenase in sea anemones to enzymes increasingly specific for the substrates L-arginine and pyruvate only. This trend is correlated with an increasing importance of ODH in glycolytic redox balance in working muscle and an increased dependence on muscle arginine phosphate reserves for rapid energy generation in higher invertebrate groups.

Item Type:	Publication - Article
Subjects:	Ecology and Environment Marine Sciences Zoology
Divisions:	Marine Biological Association of the UK > Other (MBA)
Depositing User:	Professor Paul Dando
Date made live:	06 Jan 2022 15:57
Last Modified:	06 Jan 2022 15:57
URI:	https://plymsea.ac.uk/id/eprint/9499

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