Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Co2+ | complete irreversible inhibition at 0.2 mM | Sus scrofa | |
Cu2+ | complete irreversible inhibition at 0.2 mM | Sus scrofa | |
Fe2+ | complete irreversible inhibition at 0.2 mM | Sus scrofa | |
iodoacetic acid | 55% inhibition at 0.25 mM | Sus scrofa | |
Li+ | complete inhibition at 0.2 mM | Sus scrofa | |
Mn2+ | complete irreversible inhibition at 0.2 mM | Sus scrofa | |
additional information | no inhibition by DTT, PMSF, Na2SO4, Mg2+, Ca2+, Na+, and EDTA | Sus scrofa | |
N-ethylmaleimide | 50% inhibition at 0.25 mM | Sus scrofa | |
Zn2+ | complete irreversible inhibition at 0.2 mM | Sus scrofa |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
soluble | the enzyme PNAD does not contain disulfide bridges and exists as a soluble enzyme in monomeric form | Sus scrofa | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
33000 | - |
1 * 33000, SDS-PAGE | Sus scrofa |
34000 | - |
native enzyme, gel filtration | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Sus scrofa | intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw | ? | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | Sus scrofa | - |
N-terminal L-aspartyl-[protein] + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme 11515fold to homogeneity from liver by anion exchange chromatography, ammonium sulfate fractionation, gel filtration, and another step of anion exchange chromatgraphy, follwed by chromatofocusing and again gel filtration | Sus scrofa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw | Sus scrofa | ? | - |
? | |
additional information | enzyme PNAD does not act on internal asparagine residues and requires a free Nalpha-amino groups. It has reduced or no activity on NH2-terminal asparagine dipeptides and no activity toward free asparagine or asparagine amide. It does not act on any NH2-terminal glutamine substrates | Sus scrofa | ? | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | - |
Sus scrofa | N-terminal L-aspartyl-[protein] + NH3 | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | the enzyme specifically converts NH2-terminal asparagine residues of peptide and protein substrate to aspartic acid | Sus scrofa | N-terminal L-aspartyl-[protein] + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 33000, SDS-PAGE | Sus scrofa |
More | enzyme amino acid composition, overview | Sus scrofa |
Synonyms | Comment | Organism |
---|---|---|
PNAD | - |
Sus scrofa |
protein NH2-terminal asparagine deamidase | - |
Sus scrofa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Sus scrofa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Sus scrofa |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in the N-end rule-mediated degradation in eukaryotic cells, pathway overview | Sus scrofa |
physiological function | conversion of the resulting NH2-terminal asparagine to aspartic acid by enzyme PNAD renders the protein susceptible to arginylation, polyubiquitinylation and degradation as specified by the N-end rule. Proteins beginning with Met-Asp, Met-Glu, and Met-Asn sequences are Nalpha-acetylated, while those beginning with Met-Gln sequences are not. The enzyme protein NH2-terminal asparagine deamidase (PNAD) catalyzes the specific deamidation of peptide-bound NH2-terminal asparagine residues | Sus scrofa |