Abstract
Various aquatic invertebrates including crustaceans and some bivalve mollusks contain a copious amount of free d-alanine in their tissues. In these invertebrates, d-alanine is largely accumulated with the l-form under a high-salinity environment for maintaining cell volume. d-Alanine is a major osmolyte in these invertebrate tissues, together with glycine, l-alanine, l-glutamine, and l-proline, and is responsible for intracellular isosmotic regulation. Alanine racemase, catalyzing the interconversion of d- and l-amino acids, has been isolated to homogeneity from the muscle of black tiger prawn, and its cDNA has been cloned from the muscle and hepatopancreas of kuruma prawn Marsupenaeus japonicus. This is the first time cloning was achieved in eukaryotes other than yeast. Common carp Cyprinus carpio is an omnivorous fish that often feeds on crustaceans and mollusks containing free d-alanine, but that contains only a trace amount of d-alanine in their tissues. A cDNA of d-amino acid oxidase has been cloned from carp hepatopancreas. Carp d-amino acid oxidase is an inducible enzyme. The activity and mRNA levels of d-amino acid oxidase increase in the intestine and are followed by the hepatopancreas and the kidney. Carp d-amino acid oxidase is structurally similar to the porcine kidney enzyme but is enzymatically similar to the yeast enzyme. d-Amino acid oxidase is thought to be an important enzyme responsible for the efficient utilization of the carbon skeleton of food-derived d-alanine.
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Yoshikawa, N., Sarower, M.G., Abe, H. (2016). Alanine Racemase and d-Amino Acid Oxidase in Aquatic Animals. In: Yoshimura, T., Nishikawa, T., Homma, H. (eds) D-Amino Acids. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56077-7_17
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