Substrate specificities of octopine dehydrogenases from marine invertebrates
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 broadl...
Published in: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry |
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ftplymouthml:oai:plymsea.ac.uk:9499 2023-05-15T15:22:35+02:00 Substrate specificities of octopine dehydrogenases from marine invertebrates Storey, Kenneth B. Dando, Paul R. 1982 http://plymsea.ac.uk/id/eprint/9499/ https://doi.org/10.1016/0305-0491(82)90069-4 unknown Storey, Kenneth B.; 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 <https://doi.org/10.1016/0305-0491(82)90069-4> Ecology and Environment Marine Sciences Zoology Publication - Article PeerReviewed 1982 ftplymouthml https://doi.org/10.1016/0305-0491(82)90069-4 2022-09-13T05:49:58Z 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. Article in Journal/Newspaper Arctica islandica Plymouth Marine Science Electronic Archive (PlyMSEA - Plymouth Marine Laboratory, PML) Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 73 3 521 528 |
institution |
Open Polar |
collection |
Plymouth Marine Science Electronic Archive (PlyMSEA - Plymouth Marine Laboratory, PML) |
op_collection_id |
ftplymouthml |
language |
unknown |
topic |
Ecology and Environment Marine Sciences Zoology |
spellingShingle |
Ecology and Environment Marine Sciences Zoology Storey, Kenneth B. Dando, Paul R. Substrate specificities of octopine dehydrogenases from marine invertebrates |
topic_facet |
Ecology and Environment Marine Sciences Zoology |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Storey, Kenneth B. Dando, Paul R. |
author_facet |
Storey, Kenneth B. Dando, Paul R. |
author_sort |
Storey, Kenneth B. |
title |
Substrate specificities of octopine dehydrogenases from marine invertebrates |
title_short |
Substrate specificities of octopine dehydrogenases from marine invertebrates |
title_full |
Substrate specificities of octopine dehydrogenases from marine invertebrates |
title_fullStr |
Substrate specificities of octopine dehydrogenases from marine invertebrates |
title_full_unstemmed |
Substrate specificities of octopine dehydrogenases from marine invertebrates |
title_sort |
substrate specificities of octopine dehydrogenases from marine invertebrates |
publishDate |
1982 |
url |
http://plymsea.ac.uk/id/eprint/9499/ https://doi.org/10.1016/0305-0491(82)90069-4 |
genre |
Arctica islandica |
genre_facet |
Arctica islandica |
op_relation |
Storey, Kenneth B.; 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 <https://doi.org/10.1016/0305-0491(82)90069-4> |
op_doi |
https://doi.org/10.1016/0305-0491(82)90069-4 |
container_title |
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry |
container_volume |
73 |
container_issue |
3 |
container_start_page |
521 |
op_container_end_page |
528 |
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1766353224340602880 |