Opine oxidoreductases in brachiopods, bryozoans, phoronids and molluscs
Document Type
Article
Date of Original Version
7-5-1991
Abstract
The opine dehydrogenases catalyse the reductive condensation of pyruvate with various amino acids to form products resembling octopine (N-carboxyethyl arginine). They are widely distributed among marine invertebrates and function in metabolism in the place of lactate dehydrogenase, which often has very low activity, especially in molluscs. The reaction of pyruvate, both alone and with either alanine, arginine, β-alanine, or taurine, catalysed by tissue extracts of various species, was measured by decrease in absorbance of NADH. The 27 species examined were brachiopods, bryozoans, phoronids and a wide variety of molluscs, including a scaphopod, two chitons and species representing the five subclasses of bivalves and three orders of prosobranch gastropods. Activities were coded 0-5, with 5 assigned to rates greater than 5 μmol min -1 g--1. These numbers were entered by species into a program that performed average linkage cluster analysis. Results of this analysis were transformed intoa dendrogram. The plesiomorphic state was defined as the presence of the total array of opine enzymes and the loss of one or more during evolution was taken as apomorphic. The resulting dendrogram has some features in common with standard phylogenetic trees based on morphology and development. © 1991.
Publication Title, e.g., Journal
Biochemical Systematics and Ecology
Volume
19
Issue
4
Citation/Publisher Attribution
Hammen, Carl S., and Robert C. Bullock. "Opine oxidoreductases in brachiopods, bryozoans, phoronids and molluscs." Biochemical Systematics and Ecology 19, 4 (1991): 263-269. doi: 10.1016/0305-1978(91)90013-P.