Hoyt J C, Robertson E F, Berlyn K A, Reeves H C
Department of Microbiology, Arizona State University, Tempe 85287.
Biochim Biophys Acta. 1988 Jul 14;966(1):30-5. doi: 10.1016/0304-4165(88)90125-0.
The glyoxylate cycle was first discovered during studies on bacteria and fungi with the ability to grow on acetate or ethanol as the sole carbon source. Isocitrate lyase, the first enzyme unique to the glyoxylate cycle, has been studied in numerous prokaryotic and eukaryotic organisms. However, information on this enzyme from Escherichia coli is limited. We have recently reported the purification and in vitro phosphorylation of this enzyme. In the present study we have examined and characterized a variety of inhibitors, the divalent cation requirement and the amino acid composition of E. coli isocitrate lyase and compared these results to those obtained with other organisms.
乙醛酸循环最初是在对能够以乙酸盐或乙醇作为唯一碳源生长的细菌和真菌的研究中发现的。异柠檬酸裂解酶是乙醛酸循环中首个独特的酶,已在众多原核生物和真核生物中得到研究。然而,关于大肠杆菌中这种酶的信息有限。我们最近报道了该酶的纯化及体外磷酸化。在本研究中,我们检测并表征了多种抑制剂、二价阳离子需求以及大肠杆菌异柠檬酸裂解酶的氨基酸组成,并将这些结果与其他生物的结果进行了比较。