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Literature summary for 3.5.1.114 extracted from

  • Tsirulnikov, K.; Abuladze, N.; Vahi, R.; Hasnain, H.; Phillips, M.; Ryan, C.; Atanasov, I.; Faull, K.; Kurtz, I.; Pushkin, A.
    Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein (2012), FEBS Lett., 586, 3799-3804.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.114

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged enzyme in Escherichia coli, recombinant expression of N-terminally Strep(II)-tagged enzyme Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm the enzyme associates with lipid droplets Mus musculus 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus the enzyme directly binds to the hepatitis C virus core protein and also reveals a weak endopeptidase activity towards the N-terminus of hepatitis C virus core protein, interaction analysis of the enzyme with N-terminal peptides derived from hepatitis C virus core protein via surface plasmon resonance method, overview ?
-
 ?
Nalpha-acetylated peptide + H2O Mus musculus N-terminal peptides derived from hepatitis C virus core protein acetate + peptide
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q91XE4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
blood lower expression level Mus musculus
-
brain lower expression level Mus musculus
-
kidney predominant expression Mus musculus
-
liver lower expression level Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme directly binds to the hepatitis C virus core protein and also reveals a weak endopeptidase activity towards the N-terminus of hepatitis C virus core protein, interaction analysis of the enzyme with N-terminal peptides derived from hepatitis C virus core protein via surface plasmon resonance method, overview Mus musculus ?
-
 ?
Nalpha-acetylated peptide + H2O N-terminal peptides derived from hepatitis C virus core protein Mus musculus acetate + peptide
-
 ?

Synonyms

Synonyms Comment Organism
AA3
-
 Mus musculus
aminoacylase 3
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mus musculus

General Information

General Information Comment Organism
physiological function the enzyme mediates deacetylation of N-acetyl aromatic amino acids and mercapturic acids. Deacetylation of mercapturic acids of exo- and endobiotics are likely involved in their toxicity Mus musculus