Abstract
Subcellular localization and some enzymatic properties of alanine aminotransferase (A1AT, EC 2.6.1.2) were investigated with regard to salinity-related changes in amino acid metabolism. Activities of AlAT were detected in both the cytosolic (cAlAT) and mitochondrial (mAlAT) fractions prepared from the gill tissue of the brackish-water bivalve Corbicula japonica. The cAlAT and mAlAT were partially purified and characterized with respect to their pH-dependency and K m values for the respective substrates in both directions of the A1AT reaction, pyruvate-forming and alanine-forming. These two enzymes differed from each other in the ratios of the pyruvate-forming vs. the alanine-forming activity and K m values for glutamate. The K m values for alanine were smaller than its intracellular concentration indicating that both the mAlAT and cAlAT may be physiologically functional in the pyruvate-forming direction. The A1AT is indicated to be involved in low salinity-induced decrement of intracellular alanine concentration.
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