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细菌菌株WoG13在发酵性戊二酸降解过程中的能量守恒

Energy conservation in fermentative glutarate degradation by the bacterial strain WoG13.

作者信息

Matthies C, Schink B

机构信息

Lehrstuhl Mikrobiologie I, Universität Tübingen, FRG.

出版信息

FEMS Microbiol Lett. 1992 Dec 15;100(1-3):221-5. doi: 10.1111/j.1574-6968.1992.tb14044.x.

Abstract

Dicarboxylic acids with 2-5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20-25 kJ mol-1) is conserved as sole source of growth energy either through sodium-pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate-fermenting bacterial strain WoG13 a glutaconyl-CoA-decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium-ion-pumping glutaconyl-CoA decarboxylase enzyme.

摘要

含有2至5个碳原子的二羧酸可被多种严格厌氧细菌的纯培养物发酵降解。这些脱羧反应中释放的少量自由能(约20 - 25 kJ/mol)通过钠泵脱羧酶或产电底物/产物转运装置作为唯一的生长能量来源被保存下来。在戊二酸发酵细菌菌株WoG13中检测到了一种谷氨酰辅酶A脱羧酶活性。该酶受抗生物素蛋白抑制,受钠离子刺激。酶活性部分与细胞质膜相关,表明能量保存是通过一种钠泵谷氨酰辅酶A脱羧酶完成的。

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