Degradation of α, ω-Diguanidinoalkanes and a Novel Enzyme, Diguanidinobutane Amidinohydrolase in Pseudomonas putida(Microbiology & Fermentation Industry)

概要

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Pseudomonas putida ATCC 12633 and some other fluorescent Pseudomonas strains utilized 1,4-diguanidinobutane (arcaine) and its homologues with 3〜7 methylene groups as sole nitrogen sources. The P. putida strain produced a novel enzyme which hydrolyzed 1,4-diguanidinobutane to agmatine and urea ; diguanidinobutane amidinohydrolase (EC class 3.5.3.) was proposed as the name for this enzyme. This enzyme hydrolyzed diguanidinoalkanes with 3〜10 methylene groups ; higher reaction rates were observed with 1,4-diguanidinobutane, 1,5-diguanidinopentane, and 1,6-diguanidinohexane. The enzyme was also active toward agmatine, although the rate was below 1% of that toward 1,4-diguanidinobutane, and it was suggested to catalyze the hydrolysis of the higher homologues of agmatine at higher rates. The enzyme was induced by α, ω-diguanidinoalkanes with 3〜7 methylene groups. The substrate specificities of the enzymes individually induced by the diguanidinoalkanes with 3〜7 methylene groups were very close to each other. It was then concluded that only one enzyme was produced to catalyze the initial step of the degradation of the diguanidinoalkanes commonly.
社団法人日本農芸化学会の論文
1989-11-23