Triosephosphate isomerase (TPI) (TPI)

Triosephosphate isomerase (TPI) in Cutibacterium acnes is a fundamental enzyme in the glycolytic pathway, responsible for the rapid interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate (UniProt: P0C100). This reaction is vital for the bacterium's energy production and carbon flux, supporting its survival and colonization of human skin, particularly within the anaerobic environment of sebaceous follicles (PubMed: 25100512). As C. acnes is a primary driver of the inflammatory skin condition acne vulgaris, its metabolic enzymes like TPI are explored as potential targets for novel antimicrobial therapies (PubMed: 30235833). Targeting TPI would theoretically disrupt the bacterium's ability to generate ATP, leading to growth inhibition or cell death. However, a major hurdle in developing drugs against this target is the high degree of structural conservation between bacterial TPI and the human ortholog (PubMed: 21513776). Unselective inhibition could lead to significant host toxicity, including hemolytic anemia and neurological impairment, which are characteristic of human TPI deficiency. Currently, no clinical drugs are approved that specifically target this enzyme in C. acnes, though it remains a subject of interest in metabolic profiling and antimicrobial research.

Other names

TIMTriose-phosphate isomerasePhosphotriose isomerase

Inhibition of the catalytic interconversion of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate, leading to the disruption of energy metabolism and bacterial growth.