Hydroxypyruvate isomerase (HYI)

Hydroxypyruvate isomerase (HYI) is an enzyme that catalyzes the reversible conversion of hydroxypyruvate to 2-hydroxy-3-oxopropanoate, participating in glyoxylate and dicarboxylate metabolic pathways[3][2]. It is classified as an isomerase—specifically, an aldose-ketose-isomerase (EC 5.3.1.22)[3]. In humans, HYI may play a role in carbohydrate transport and metabolism and is implicated in the regulation of fibroblast functions through interactions with the protein P311, which is relevant for wound healing and hypertrophic scar formation[2]. Despite these molecular roles, HYI is primarily annotated as a putative enzyme with no confirmed disease associations or therapeutic interventions targeting it. No drugs or medical biomarkers are currently linked to HYI. The enzyme's molecular structures adopt TIM barrel folds and are predicted to have conserved active sites suitable for isomerase activity[1]. While theoretical therapeutic relevance exists in fibrosis/scarring pathways, HYI is not an established or clinically actionable target based on current evidence[2][3][4].

Other names

Putative hydroxypyruvate isomeraseHYIHT036SB156Endothelial cell apoptosis protein E-CE1Hydroxypyruvate isomerase homolog

For enzyme activity: Catalyzes intramolecular oxidoreduction (aldose-ketose isomerization) of hydroxypyruvate For biological modulation: May influence fibroblast proliferation, migration, and extracellular matrix production by modulating P311 interaction (therapeutic mechanism not established)