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• W2326714605 abstract "Two types of dried cell preparations of Bact. succinicum were prepared, one having the activity of acetate oxidation and the other loosing the activity of acetate oxidation almost completely. By using the latter preparation, the author found that all the acids belonging to tricarboxylic acid cycle (TCA-cycle except _??_ ketoglutarate were rapidly oxidized to acetate (Table 1, Fig 1 and 2). Since the oxidation of each one mole of these substrates stopped at the stage of one mole of acetate, it is very favorable that the oxidation takes place via TCA cycle. From the above results and some additional evidences (see Table 2), it is probable that if _??_ ketoglutarate is the member of TCA-cycle in this bacteria, the permeability of the preparation limits the oxidation. It was found that _??_-dipyridyl, which had been proved by the authors to inhibit the anaerobic decomposition of citrate, also inhibits the oxidation of l-malate, pyruvate and acetate (Table 4). It was clearly demonstrated that the agent inhibited pyruvate oxidase system and at the same time either the activation of acetate or the condensing enzyme. It was found that a new inhibitor d-malate inhibits almost completely the acetate oxidation at rather dilute concentration (M/900), while the oxidation of citrate to acetate was quite stable to d-malate (Fig. 6, 7 and 8). Probably d-malate inhibits the condensing enzyme competing with, oxaloacetate. From the inhibition experiements above cited the mechanism of citrate, breakdown in Bact. succinicum may be summarized as follows _??_ Dotted lines represent the inhibition by the agents described. In aerobic condition, citrate is oxidized exclusively via TCA-cycle, because _??_-dipyridyl does not inhibit the aerobic oxidation of citrate. In anaerobic condition, citrate is decomposed to acetate and oxaloacetate by the condensing enzyme(?), some part of the latter compound is reduced to succinate coupled with the oxidation of citrate to succinate via TCA-cycle. There are some evidences that the condensing enzyme is not responsible for the anaerobic breakdown of citrate, since the preparation aged thirty days or more which cantains both the activity of acetate oxidation and all enzym systems belonging to TCA-cycle, does not decompose citrate anaerobically at a detectable rate. Thus it is concluded that either some cofactor (s?) which is not necessary for the oxidation of acetate plays an important role in the breakdown of citrate, or the enzyme different from condensing enzyme is responsible for the anaerobic decomposition of citrate." @default.
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• W2326714605 date "1953-01-01" @default.
• W2326714605 modified "2023-10-02" @default.
• W2326714605 title "Studies on the Decomposition of Citrate by Microörganisms" @default.
• W2326714605 doi "https://doi.org/10.1271/nogeikagaku1924.27.832" @default.
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