Succinate-semialdehyde Dehydrogenase for L-Arginine and Putrescine Degradation in Brevibacterium helvolum(Microbiology & Fermentation Industry)

概要

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Succinate-semialdehyde dehydrogenase (EC 1.2.1.16) was purified to apparent homogeneity from L-arginine-grown cells of Brevibacterium helvolum IFO 12073 (ATCC 11822). The molecular weight and the subunit molecular weight of the enzyme were approximately 250,000 and 59,000, respectively, suggesting that the enzyme is a tetramer of identical subunits. The apparent Michaelis constant (Km) for succinate-semialdehyde was approximately 30μ_M. The enzyme used both NAD^+ and NADP^+ as the coenzyme almost equally. The apparent Km values for NAD^+ and NADP^+ were 0.5 m_M and 0.15m_M, respectively. The maximum reaction rate (V_<max>) of about 110μmol/min/mg was shown with NAD^+ and a very close value was obtained with NADP^+ . Malonate-semialdehyde and other aldehydes tested were inert as substrates. The optimum pH was 9.0-9.5. The enzyme was sensitive to sulfhydryl reagents.
社団法人日本農芸化学会の論文
1991-01-23