Asparaginase-like protein 1 (ASRGL1)

Asparaginase-like protein 1 (ASRGL1) is a human enzyme in the N-terminal nucleophile (Ntn) hydrolase family that displays both L-asparaginase and beta-aspartyl peptidase activity[1][2][3]. It is processed by autocleavage into alpha and beta chains, forming an active heterodimer. ASRGL1 catalyzes the conversion of L-asparagine to L-aspartate and participates in the hydrolysis of beta-aspartyl dipeptides, potentially contributing to protein repair and the prevention of accumulation of isoaspartyl-containing peptides, which are toxic to mammalian cells[1]. Highest expression is seen in the brain, testis, and reproductive tissues, and the enzyme is localized mainly to the cytoplasm and microtubules[2]. Clinically, loss of ASRGL1 is associated with worse prognosis in endometrial cancer[2], but unlike bacterial asparaginase, the human enzyme has not been directly targeted by approved drugs.

Other names

Asparaginase and isoaspartyl peptidase 1Isoaspartyl peptidase/L-asparaginaseIsoaspartyl peptidase/L-asparaginase alpha chainIsoaspartyl peptidase/L-asparaginase beta chainALPALP1CRASHFLJ22316Asparaginase-like protein 1Beta-aspartyl-peptidaseIsoaspartyl dipeptidaseL-asparagine amidohydrolaseTestis secretory sperm-binding protein Li 242mP

Not established for approved drugs, since no drugs are known to selectively target ASRGL1 in clinical use. Theoretically, an inhibitor or activator would modulate L-asparaginase and/or beta-aspartyl peptidase activity, influencing L-asparagine or isoaspartyl peptide levels.