Abstract

Pseudomonas sp. SMIC-3 grown on NMP was physiologically differentiated from that on glucose. Growth of SMIC-3 in an NMP-defined medium was approximately three times lower than that in a glucose-defined medium. Methylamine and 1-methyl succinimide were detected in culture fluid of SMIC-3 grown in an NMP-defined medium. Methylamine content in the culture fluid was very similar to NMP consumed by SMIC-3, but 1-methyl succinimide content was much less than the consumed NMP. Crude enzyme isolated from SMIC-3 grown on NMP catalyzed production of methylamine, 1-methyl succinimide, and succinate from NMP but that on glucose did not. Crude enzyme isolated from SMIC-3 grown on glucose and NMP commonly catalyzed dehydrogenation of pyruvate, isocitrate, and malate coupled to reduction of NAD+ to NADH. 2D-SDS-PAGE pattern of total soluble proteins isolated from SMIC-3 grown on glucose was significantly different from that on NMP. Physiological function of SMIC-3 for catabolizing NMP may be selectively induced and activated by NMP.

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