Isolation and Some Properties of an Aspartate Aminotransferase Inhibitor, Gostatin

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Abstract
A novel aspartate aminotransferase inhibitor named gostatin was isolated as crystals from the culture filtrate of Streptomyces sumanensis NK-23. The structure has been established to be 5-amino-2-carboxy-4-oxo-1,4,5,6-tetrahydropyridine-3-acetic acid by X-ray crystallographic analysis (K. Ibata et al., manuscript in preparation). The results of chemical and instrumental analyses of the inhibitor are described in this paper. Gostatin showed time-dependent inhibitory action against aspartate aminotransferases and alanine aminotransferase. Both pyridoxal phosphate- and pyridoxamine phosphate-linked enzymes were sensitive to the inhibitor.