Allantoicase (ALLC)

Allantoicase is an enzyme (systematic name: allantoate amidinohydrolase, EC 3.5.3.4) that catalyzes the hydrolysis of allantoate to (S)-ureidoglycolate and urea, as part of the purine degradation pathway. It belongs to the hydrolase family, specifically acting on carbon-nitrogen bonds in linear amidines. The enzyme is hexameric (dimer of trimers), with each subunit showing a jelly-roll beta-sheet motif, and the active site is formed by conserved surface patches at the interface of these motifs[1][2][4][5][7]. While important for nitrogen recycling in plants, microorganisms, fish, and amphibians, the human genome encodes a homolog (ALLC) that appears to be functionally inactive; thus, there is no established role for human disease or as a therapeutic target[1][6]. No drugs or biomarkers are currently associated with allantoicase, and there are no known safety concerns.

Other names

Allantoate amidinohydrolaseALCprobable inactive allantoicaseputative inactive allantoicaseallantoicase (EC 3.5.3.4)