Escherichia coli, the most studied prokaryote, is an excellent host for producing valuable chemicals from renewable resources as it is easy to manipulate genetically. Since the periplasmic environment can be easily controlled externally, elucidating how the localization of specific proteins or small molecules in the periplasm affects metabolism may lead to bioproduction development using E. coli. We investigated metabolic changes and its mechanisms occurring when specific proteins are localized to the E. coli periplasm. We found that the periplasmic localization of β-glucosidase promoted the shikimate pathway involved in the synthesis of aromatic chemicals. The periplasmic localization of other proteins with an affinity for glucose-6-phosphate (G6P), such as inactivated mutants of Pgi, Zwf, and PhoA, similarly accelerated the shikimate pathway. Our results indicate that G6P is transported from the cytoplasm to the periplasm by the glucose transporter protein EIICB^Glc, and then captured by β-glucosidase.

大肠杆菌是研究最多的原核生物，是从可再生资源中生产有价值化学物质的极好宿主，因为它很容易进行基因操作。由于周质环境可以很容易地从外部控制，阐明特定蛋白质或小分子在周质中的定位如何影响新陈代谢可能会导致使用大肠杆菌进行生物生产开发。我们研究了特定蛋白质定位于大肠杆菌时发生的代谢变化及其机制周质。我们发现β-葡萄糖苷酶的周质定位促进了莽草酸途径参与芳香化学物质的合成。对葡萄糖-6-磷酸 (G6P) 具有亲和力的其他蛋白质的周质定位，例如 Pgi、Zwf 和 PhoA 的失活突变体，同样加速了莽草酸途径。我们的结果表明，G6P 通过葡萄糖转运蛋白 EIICB ^Glc从细胞质转运到周质，然后被 β-葡萄糖苷酶捕获。