원문정보
초록
영어
In Selenomonas ruminantium, strictly anaerobic and gram negative bacterium, cadaverine and putrescine, which are essential constituents of the peptidoglycan, are synthesized from L-lysine and L-ornithine by a constitutive lysine/ornithine decarboxylase (LDC/OCD). In this, firstly, we showed that S. ruminantium converted L-arginine into putrescine via agmatine. Secondary, we purified and characterized arginine decarboxylase, the key enzyme in agmatine pathway for putrescine synthesis. Arginine decarboxylase was purified about 2,030-fold to electrophoretic homogeneity with a specific activity of 0.25 kat/kg of protein. The N-terminal amino acid sequence of the enzyme was M1DRINQHTAP10VYEAMLELRKRR22. The apparent molecular mass of the purified ADC preparation was 120 kDa as judged by gel filteration analysis, and 58 kDa on SDS-PAGE. The Km value for L-arginine and L-lysine were 5.6 mM and 50 mM, respectively.