Tissue-specific forms of alanopine and strombine dehydrogenases were detected in the bivalve mollusc, Mercenaria mercenaria (Linn.), by isoelectrofocusing. Alanopine dehydrogenase had a pI of 5.0-5.25 and predominated in the gill and mantle while strombine dehydrogenase had a pI of 4.75-4.80 and predominated in the adductor and foot muscles. The enzymes from gill and foot muscle were partially purified, about 20-fold each, to final specific activities of 3 and 37μmol·min-1·mgprotein-1, respectively. The alanopine dehydrogenase from gill had a much higher affinity for alanine (apparent Km = 28±2.1mM) than for glycine (apparent Km = 291±40 mM) and showed substantial activity with a variety of other neutral L-amino acids. The strombine dehydrogenase from foot muscle had similar affinities for alanine and glycine (apparent Kmvalues were 242±11 and 173±1.3 mM, respectively) but apart from these two amino acids and L-2-aminobutyrate showed a restricted use of other L-amino acids. Affinities for pyruvate were comparable for both enzymes (Kmvalues were0.38±0.05mM and 0.32±0.04 mM for the gill alanopine dehydrogenase and foot muscle strombine dehydrogenase, respectively). Both enzymes function as the terminal dehydrogenase of glycolysis in their respective tissues and have roles in maintaining energy production under the stresses of environmental (low-tide exposure) or functional (burst muscle work) anoxia. The distribution of the two enzyme types, coupled with the glycine (8.0 and 2.9μmol·gwetwt-1 in foot and gill) and alanine (18.9 and 3.8μmol·g-in foot and gill) contents of the two tissues, accounts for the dominance of alanopine in soft tissues of the clam and the appearance of near equal amounts of the two imino acids in muscles.

Additional Metadata
Keywords Alanopine dehydrogenase, Anaerobic metabolism, Mercenaria mercenaria, Strombine dehydrogenase
Persistent URL dx.doi.org/10.1016/0022-0981(87)90170-5
Journal Journal of Experimental Marine Biology and Ecology
Fields, J.H.A. (Jeremy H.A.), & Storey, K. (1987). Tissue-specific alanopine dehydrogenase from the gill and strombine dehydrogenase from the foot muscle of the cherrystone clam Mercenaria mercenaria (Linn.). Journal of Experimental Marine Biology and Ecology, 105(2-3), 175–185. doi:10.1016/0022-0981(87)90170-5