Acireductone dioxygenase 1 (ADI1)

Acireductone dioxygenase 1 (ADI1) is a metal-dependent enzyme in the methionine salvage pathway ("MTA cycle"), crucial for recycling methionine from methylthioadenosine. It belongs to the cupin superfamily and can bind iron or nickel at its catalytic center, affecting its substrate and product profile. Beyond its canonical enzymatic role, ADI1 is multifunctional: it acts as a tumor suppressor (proapoptotic and antiproliferative) in prostate and liver cancer, and can influence the epigenome by increasing S-adenosylmethionine levels, thus globally affecting promoter methylation and gene expression. ADI1 further participates in modulating mRNA processing through nuclear localization and has roles in viral infection, notably by facilitating hepatitis C virus entry through interactions with cell surface proteins. Its diverse subcellular localizations and tissue-specific activities underscore its pleiotropic functions, highlighting its utility as a potential biomarker for cancer and as a putative, though as-yet-unexploited, therapeutic target.

Other names

Acireductone dioxygenaseMTCBP1HMFT1638ARD'Fe-ARDARDNi-ARDMTCBP-1Sip-LSIPLAPL1FLJ10913mtnDAcireductone dioxygenase (Fe(2+)-requiring)Acireductone dioxygenase (Ni(2+)-requiring)Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1Submergence-induced protein-like factorMT1-MMP cytoplasmic tail-binding protein-1submergence induced protein 2

Not applicable directly, as no known drugs directly targeting ADI1 exist. Enzyme inhibition or modulation would hypothetically impact methionine salvage and methylation landscape, but this remains theoretical.