Identification of YigL as a PLP/PNP phosphatase in Escherichia coli.

ABSTRACT: In various organisms, the coenzyme form of vitamin B₆, pyridoxal phosphate (PLP), is synthesized from pyridoxine phosphate (PNP). Control of PNP levels is crucial for metabolic homeostasis because PNP has the potential to inhibit PLP-dependent enzymes and proteins. Although the only known pathway for PNP metabolism in Escherichia coli involves oxidation by PNP oxidase, we detected a strong PNP phosphatase activity in E. coli cell lysate. To identify the unknown PNP phosphatase(s), we performed a multicopy suppressor screening using the E. coli serA pdxH strain, which displays PNP-dependent conditional lethality. The results showed that overexpression of the yigL gene, encoding a putative sugar phosphatase, effectively alleviated the PNP toxicity. Bioc

SUBMITTER: Matsuo H 

PROVIDER: S-EPMC11409668 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature