Succinate Semialdehyde Dehydrogenase of Rhodopseudomonas spheroides which is Active with Both NADP⁺ and NAD⁺

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Succinate semialdehyde dehydrogenase [EC 1. 2. 1. 16] was purified from Rhodopseudomonas spheroides about 250 fold. The succinate semialdehyde dehydrogenase in R. spheroides was active both with NADP⁺ and with NAD⁺. The K_m value for NAD⁺ (O.8 mM) was much larger than that for NADP⁺ (0.06mM), while the K_m value for succinate semialdehyde measured with NAD⁺ was identical with that measured with NADP⁺. The V_max obtained with NAD⁺ was considerably larger than that obtained with NADP⁺, and the pH optima with these electron acceptors were very close to each other.