LACTATE AND GLUCOSE OXIDATION SYSTEMS IN ACETOBACTER SUBOXYDANS
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概要
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1. From a strain of Acetobacter suboxydans, a glucose and a lactic enzytne were obtained in cell-free states. The lactic enzyme shows as strong activity as the glucose enzyme but is more stable than the latter toward various purification procedures : both are sensitive to high temperature treatment. Activities of the two enxymes and the MICHAELIS constants of the glucose enzyme were determined under both aerobic and anaerobic conditions. 2. Carbon monoxide inhibits the oxygen-uptake in both glucose and lactate oxidation. WARBURG's distribution constant for lactate oxidation is 6.7. These results suggest the participation of an heme enzyme in the oxidation system. Effects of copper reagents, narcotics and PCMB were also examined. 3. The dehydrogenase activities (reduction of dye) of the enzymes are more sensitive to high temperature than the corresponding activities in oxygen-uptake. 4. By combining a dehydrogenase preparation which has lost its oxygen-absorbing activity through acetone treatment, with a heated extract, a partial recovery of oxygen-uptake can be realized in lactate oxidation. 5. L-Cysteine is utilized as hydrogen donor by the bacterium. This oxidative reaction, unlike the oxidation of lactate, is not inhibited by surface active reagents.
- 日本植物生理学会の論文
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関連論文
- COMPONENTS OF THE ELECTRON-TRANSFERRING SYSTEM IN ACETOBACTER SUBOXYDANS AND RECONSTRUCTION OF THE LACTATE OXIDATION SYSTEM
- LACTATE AND GLUCOSE OXIDATION SYSTEMS IN ACETOBACTER SUBOXYDANS