Strombine [N--(carboxymethyl)-D-alanine] dehydrogenase and alanopine {meso-N-(1-carboxymethyl)-alanine} dehydrogenase from the mussel Mytilus edulis.

DANDO, P. R.. 1981 Strombine [N--(carboxymethyl)-D-alanine] dehydrogenase and alanopine {meso-N-(1-carboxymethyl)-alanine} dehydrogenase from the mussel Mytilus edulis.. Biochemical Society Transactions, 9 (4). 297-298. https://doi.org/10.1042/bst0090297

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Abstract/Summary

The mussel Mvtilus edulis L. has at least four NAD oxidoreductases competing for pyruvate as a substrate (Storey et al., 1981), namely D-lactate dehydrogenase (EC 1.1. 1.28), octopine dehydrogenase (EC 1.5. 1.1 I), alanopine dehydrogenase [meso-N-(1-carboxyethyl) alanine: NAD+ oxidoreductasel and strombine dehydrogenase I N- (carboxymethy1)-D-alanine: NAD+ oxidoreductasel. Some properties of lactate dehydrogenase (Hammen, 1975) and octopine dehydrogenase (Gade, 1980) from Mytilus edulis have been described. Strombine dehdrobenase occurs in the adductor muscle and also catalyses alanopine formation (Storey et al. 1981). Ihave partially purified alanopine dehydrogenase fronm the foot and strombine dehydrogenase from the anterior adductor muscleof Mytilis and have studied some oftheir properties.

Item Type: Publication - Article
Subjects: Marine Sciences
Divisions: Marine Biological Association of the UK > Other (MBA)
Depositing User: Professor Paul Dando
Date made live: 09 Aug 2022 13:10
Last Modified: 09 Aug 2022 13:10
URI: http://plymsea.ac.uk/id/eprint/9758

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