Aldehyde dehydrogenase 16 family member A1 (ALDH16A1)

Aldehyde dehydrogenase 16 family member A1 (ALDH16A1) is an atypical member of the aldehyde dehydrogenase (ALDH) superfamily. Unlike canonical ALDH enzymes, mammalian ALDH16A1 is catalytically inactive due to the loss of a critical active-site cysteine residue, and consequently, it does not exhibit typical aldehyde-processing activity. Nevertheless, it retains two ALDH domains and possesses several transmembrane and coiled-coil motifs, making it distinct among ALDH family proteins[1][2]. ALDH16A1 is highly expressed in the kidney and liver, where it appears to play a regulatory role in uric acid homeostasis, likely by interacting with the enzyme hypoxanthine–guanine phosphoribosyltransferase (HPRT1), modulating urate metabolism. Rare missense variants in ALDH16A1 have been associated with hyperuricemia and gout susceptibility. Additionally, ALDH16A1 interacts with maspardin, linking it to Mast syndrome, a form of hereditary spastic paraplegia. Emerging research also suggests potential non-catalytic roles in tumor biology (e.g., cell proliferation, migration, and epithelial–mesenchymal transition), and in lipid metabolism. Overall, ALDH16A1 acts primarily through protein–protein interactions rather than enzymatic activity[1][2][3][4][5].

Other names

ALDH16A1Aldehyde dehydrogenase family 16 member A1MGC10204

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