作者: Chulwoo Park , Bora Shin , Woojun Park
DOI: 10.1038/S41598-019-50852-3
关键词: Lactate dehydrogenase 、 Isocitrate lyase 、 Wild type 、 Malate synthase 、 Escherichia coli 、 Mutant 、 Biochemistry 、 Glyoxylate cycle 、 Chemistry 、 Metabolism
摘要: The glyoxylate shunt (GS), involving isocitrate lyase (encoded by aceA) and malate synthase G glcB), is known to play important roles under several conditions including oxidative stress, antibiotic defense, or certain carbon source metabolism (acetate fatty acids). Comparative growth analyses of wild type (WT), aceA, glcB null-strains revealed that but not glcB, essential for cells grow on either acetate (1%) hexadecane in Acinetobacter oleivorans DR1. Interestingly. the aceA knockout strain was able slower 0.1% than parent strain. Northern Blot analysis showed expression dependent concentration H2O2, while constitutively expressed. Up-regulation stress response-related genes down-regulation main metabolism-participating a ΔaceA mutant, compared strain, suggested an mutant susceptible toxicity, grows slowly acetate. However, ΔglcB no defect susceptibility suggesting presence alternative pathway eliminate toxicity. A lactate dehydrogenase (LDH, encoded ldh) could possibly mediate conversion from oxalate based our RNA-seq profiles. Oxalate production during degradation impaired ΔldhΔglcB double both hexadecane-supplemented media LDH potential detoxifying enzyme glyoxylate. Our constructed LDH-overexpressing Escherichia coli also role lactate, acetate, metabolisms. E. produced condition. In conclusion, GS player, pathways exist A.