Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position.
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N-terminal asparagine amidohydrolase; PNAA; PNAD; protein N-terminal Asn amidase; protein N-terminal asparagine amidase; Protein N-terminal asparagine amidohydrolase; Protein NH2-terminal asparagine amidohydrolase; Protein NH2-terminal asparagine deamidase; protein NTN-amidase