Protein N-terminal asparagine amidase (NTAN1)

Protein N-terminal asparagine amidase (NTAN1) is an enzyme that catalyzes the conversion (deamidation) of N-terminal asparagine residues to aspartate on substrate proteins, a key step in the eukaryotic N-end rule pathway of targeted protein degradation. NTAN1 exhibits high specificity for N-terminal Asn, preferring substrates with hydrophobic second-position residues, and functions via a CNF1/YfiH-like cysteine hydrolase fold with a conserved catalytic triad. Once deamidated, the N-terminal aspartate undergoes arginylation and subsequent ubiquitin-dependent proteasomal degradation. NTAN1 activity is implicated in maintenance of cellular protein turnover and normal neurological function, with genetic variants associated with certain diseases. There are currently no known drugs targeting NTAN1 directly[1][2][3][5].

Other names

Protein N-terminal Asn amidasePNAAPNADprotein NH2-terminal asparagine amidohydrolaseprotein NH2-terminal asparagine deamidaseprotein NTN-amidase

(For hypothetical drugs): Inhibition or modulation of NTAN1 would block the deamidation of N-terminal Asn, potentially altering protein stability and turnover via the N-end rule pathway