Structural highlights
Function
[NTAN1_HUMAN] N-terminal asparagine deamidase that mediates 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 NTAN1/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, nor on acetylated N-terminal peptidyl Asn.[1]
References
- ↑ Cantor JR, Stone EM, Georgiou G. Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. Biochemistry. 2011 Apr 12;50(14):3025-33. doi: 10.1021/bi101832w. Epub 2011 Mar, 18. PMID:21375249 doi:http://dx.doi.org/10.1021/bi101832w
