Phenylalanine-specific permease (PheP) (PheP)

Phenylalanine-specific permease (PheP) is a high-affinity membrane transporter primarily characterized in bacteria such as Escherichia coli (1, 8). It belongs to the amino acid-polyamine-organocation (APC) family and functions as a proton-coupled symporter, utilizing the proton motive force to actively transport L-phenylalanine and, to a lesser extent, L-tyrosine into the cytoplasm (1, 15). While PheP is not a human protein, it has emerged as a significant therapeutic component in the field of synthetic biology and live bacterial therapeutics (24, 26). Specifically, engineered strains like SYNB1618 and SYNB1934 utilize overexpressed PheP to facilitate the rapid uptake of dietary phenylalanine from the gastrointestinal tract into the bacteria, where it is subsequently degraded by enzymes like phenylalanine ammonia lyase (PAL) to treat phenylketonuria (PKU) (32, 36). Additionally, PheP is being explored as a potential antimicrobial target, as its inhibition may attenuate the growth and virulence of pathogens such as Staphylococcus aureus (25).

Other names

Phenylalanine:H(+) symporter PhePPhenylalanine-specific transport systemPhenylalanine permease

Proton-coupled symport of phenylalanine across the cell membrane