Protein NH2-terminal asparagine amidohydrolase ; PNAA ; Protein NH2-terminal asparagine deamidase ; PNAD
Categories
Elisa
Function
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.
Specificity
Natural and recombinant Human Protein N-terminal asparagine amidohydrolase
"Cloning and expression of a novel human cDNA homology to murine N-terminal asparagine amidohydrolase (Ntan1) mRNA." Jiang C.L., Yu L., Fan Y.X., Tu Q., Jiang J.X., Zhao S.Y. Submitted (2003-07) to the EMBL/GenBank/DDBJ databases
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;CATALYTIC ACTIVITY;ENZYME REGULATION;BIOPHYSICOCHEMICAL PROPERTIES;REMOVAL OF INITIATOR METHIONINE;MUTAGENESIS OF PRO-2 AND CYS-75
Reviews of ELISA Kit for Human Protein N-terminal asparagine amidohydrolase