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Literature summary extracted from

  • Pushkin, A.; Carpenito, G.; Abuladze, N.; Newman, D.; Tsuprun, V.; Ryazantsev, S.; Motemoturu, S.; Sassani, P.; Solovieva, N.; Dukkipati, R.; Kurtz, I.
    Structural characterization, tissue distribution, and functional expression of murine aminoacylase III (2003), Am. J. Physiol. Cell Physiol., 286, C848-856.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.114 expressed in HEK-293T cells Mus musculus
3.5.1.114 expression in HEK-293 cells Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.114 1.1
-
 N-acetyl-S-benzyl-L-cysteine pH 7.5, 37°C Mus musculus
3.5.1.114 1.4
-
 N-acetyl-L-tyrosine pH 7.5, 37°C Mus musculus
3.5.1.114 1.6
-
 N-acetyl-L-phenylalanine pH 7.5, 37°C Mus musculus
3.5.1.114 1.8
-
 N-acetyl-L-histidine pH 7.5, 37°C Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.114 cytoplasm predominant cytoplasmic localization of aminoacylase III Mus musculus 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.114 35000
-
 4 * 35000, the monomers of the enzyme are arranged with a fourfold rotational symmetry, SDS-PAGE Mus musculus
3.5.1.114 35188
-
 4 * 35188, calculated from sequence Mus musculus
3.5.1.114 140000
-
 gel filtration Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.114 Mus musculus Q91XE4
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.114 additional information the enzyme has consensus sites for N-glycosylation (Asn70 and Asn117), tyrosine sulfation (Tyr88, Tyr165, and Tyr272), protein kinase C (Thr298), and casein kinase II (Thr83, Ser130, Ser160, Thr201, and Ser266) phosphorylation, and myristylation (Gly18, Gly19, Gly22, Gly27, and Gly185) Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.114 brain less expression Mus musculus
-
3.5.1.114 heart less expression Mus musculus
-
3.5.1.114 kidney the enzyme is expressed predominantly in kidney, localized predominantly to the apical domain of S1 proximal tubules and the cytoplasm of S2 and S3 proximal tubules. The data suggest that in kidney proximal tubules, aminoacylase III plays an important role in deacetylating mercapturic acids Mus musculus
-
3.5.1.114 liver less expression Mus musculus
-
3.5.1.114 lung less expression Mus musculus
-
3.5.1.114 small intestine less expression Mus musculus
-
3.5.1.114 stomach less expression Mus musculus
-
3.5.1.114 testis less expression Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.114 additional information the enzyme uses as a substrate the N-acetylated L-aromatic amino acids tyrosine, phenylalanine, and tryptophan Mus musculus ?
-
 ?
3.5.1.114 N-acetyl-L-histidine + H2O
-
 Mus musculus acetate + L-histidine
-
 ?
3.5.1.114 N-acetyl-L-phenylalanine + H2O
-
 Mus musculus acetate + L-phenylalanine
-
 ?
3.5.1.114 N-acetyl-L-tyrosine + H2O
-
 Mus musculus acetate + L-tyrosine
-
 ?
3.5.1.114 N-acetyl-S-benzyl-L-cysteine + H2O
-
 Mus musculus acetate + S-benzyl-L-cysteine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.114 tetramer 4 * 35000, the monomers of the enzyme are arranged with a fourfold rotational symmetry, SDS-PAGE Mus musculus
3.5.1.114 tetramer 4 * 35188, calculated from sequence Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.5.1.114 Acy3
-
 Mus musculus
3.5.1.114 aminoacylase III
-
 Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.114 7.5
-
 substrate: N-acetyl-S-benzyl-L-cysteine Mus musculus
3.5.1.114 7.6
-
 substrate: N-acetyl-L-histidine or N-acetyl-L-tyrosine Mus musculus
3.5.1.114 7.7
-
 substrate: N-acetyl-L-phenylalanine Mus musculus

General Information

EC Number General Information Comment Organism
3.5.1.114 physiological function aminoacylase III contributes to the nephrotoxicity to cysteine S-conjugates Mus musculus