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Literature summary extracted from

  • Stewart, A.; Arfin, S.; Bradshaw, R.
    Protein NH2-terminal asparagine deamidase: isolation and characterization of a new enzyme (1994), J. Biol. Chem., 269, 23509-23517.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.121 Co2+ complete irreversible inhibition at 0.2 mM Sus scrofa
3.5.1.121 Cu2+ complete irreversible inhibition at 0.2 mM Sus scrofa
3.5.1.121 Fe2+ complete irreversible inhibition at 0.2 mM Sus scrofa
3.5.1.121 iodoacetic acid 55% inhibition at 0.25 mM Sus scrofa
3.5.1.121 Li+ complete inhibition at 0.2 mM Sus scrofa
3.5.1.121 Mn2+ complete irreversible inhibition at 0.2 mM Sus scrofa
3.5.1.121 additional information no inhibition by DTT, PMSF, Na2SO4, Mg2+, Ca2+, Na+, and EDTA Sus scrofa
3.5.1.121 N-ethylmaleimide 50% inhibition at 0.25 mM Sus scrofa
3.5.1.121 Zn2+ complete irreversible inhibition at 0.2 mM Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.121 soluble the enzyme PNAD does not contain disulfide bridges and exists as a soluble enzyme in monomeric form Sus scrofa
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.121 33000
-
 1 * 33000, SDS-PAGE Sus scrofa
3.5.1.121 34000
-
 native enzyme, gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.121 additional information Sus scrofa intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw ?
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O Sus scrofa
-
 N-terminal L-aspartyl-[protein] + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.121 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.121 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

EC Number Source Tissue Comment Organism Textmining
3.5.1.121 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.121 additional information intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw Sus scrofa ?
-
 ?
3.5.1.121 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 ?
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O
-
 Sus scrofa N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 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

EC Number Subunits Comment Organism
3.5.1.121 monomer 1 * 33000, SDS-PAGE Sus scrofa
3.5.1.121 More enzyme amino acid composition, overview Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
3.5.1.121 PNAD
-
 Sus scrofa
3.5.1.121 protein NH2-terminal asparagine deamidase
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.121 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.121 7.4
-
 assay at Sus scrofa

General Information

EC Number General Information Comment Organism
3.5.1.121 metabolism the enzyme is involved in the N-end rule-mediated degradation in eukaryotic cells, pathway overview Sus scrofa
3.5.1.121 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