G6P-capturing molecules in the periplasm of Escherichia coli accelerate the shikimate pathway

Ryosuke Fujiwara, Mariko Nakano, Yuuki Hirata, Chisako Otomo, Daisuke Nonaka, Sakiya Kawada, Hikaru Nakazawa, Mitsuo Umetsu, Tomokazu Shirai, Shuhei Noda, Tsutomu Tanaka, Akihiko Kondo

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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 EIICBGlc, and then captured by β-glucosidase.

Original languageEnglish
Pages (from-to)68-81
Number of pages14
JournalMetabolic Engineering
Publication statusPublished - 2022 Jul


  • Escherichia coli
  • Glucose-6-phosphate
  • Periplasm
  • Phosphotransferase system
  • Shikimate pathway

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


Dive into the research topics of 'G6P-capturing molecules in the periplasm of Escherichia coli accelerate the shikimate pathway'. Together they form a unique fingerprint.

Cite this