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Literature summary for 3.5.1.121 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

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

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

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

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Substrates and Products (Substrate)

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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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