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Literature summary extracted from

  • Lindner, H.A.; Alary, A.; Boju, L.I.; Sulea, T.; Menard, R.
    Roles of dimerization domain residues in binding and catalysis by aminoacylase-1 (2005), Biochemistry, 44, 15645-15651.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.14 D274A site-directed mutagenesis, the mutant shows 5695fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour Homo sapiens
3.5.1.14 H206A site-directed mutagenesis, dimerization domain mutant, the mutant shows 560fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour Homo sapiens
3.5.1.14 H206K site-directed mutagenesis, dimerization domain mutant, the mutant shows 348fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour Homo sapiens
3.5.1.14 H206N site-directed mutagenesis, dimerization domain mutant, the mutant shows 11837fold reduced activity compared to the wild-type enzyme Homo sapiens
3.5.1.14 N263D site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme Homo sapiens
3.5.1.14 N263S site-directed mutagenesis, dimerization domain mutant, the mutant shows 152fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour Homo sapiens
3.5.1.14 R276A site-directed mutagenesis, dimerization domain mutant, the mutant shows 8995fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour Homo sapiens
3.5.1.14 R276N site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme Homo sapiens
3.5.1.14 R276Q site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.14 additional information
-
 additional information steady-state kinetics of wild-type and mutant enzymes, kinetics of mutants N263D, R276N, and R276Q are not measurable Homo sapiens
3.5.1.14 0.39
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant D274A Homo sapiens
3.5.1.14 0.43
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant wild-type enzyme Homo sapiens
3.5.1.14 0.54
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206A Homo sapiens
3.5.1.14 0.58
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206K Homo sapiens
3.5.1.14 0.78
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant N263D Homo sapiens
3.5.1.14 2.02
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206N Homo sapiens
3.5.1.14 67.4
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant R276A Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.14 Zn2+ binding site structure, H206 and E146 are involved Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.14 Homo sapiens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.14 an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate active site structure, catalysis involves residues H206, N263, R276, and D274, the dimerization domain residues play important roles in binding and catalysis, overview Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.14 Nalpha-acetylmethionine + H2O
-
 Homo sapiens acetate + L-methionine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.14 More dimerization domain residues play important roles in binding and catalysis, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.1.14 Acy1
-
 Homo sapiens
3.5.1.14 aminoacylase-1
-
 Homo sapiens
3.5.1.14 More the enzyme belongs to the M20 metallopeptidase family Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.14 22
-
 assay at room temperature Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.14 additional information
-
 additional information kinetics of mutants N263D, R276N, and R276Q are not measurable Homo sapiens
3.5.1.14 0.006
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant D274A Homo sapiens
3.5.1.14 0.015
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206N Homo sapiens
3.5.1.14 0.086
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206A Homo sapiens
3.5.1.14 0.149
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206K Homo sapiens
3.5.1.14 0.458
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant N263D Homo sapiens
3.5.1.14 0.667
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant R276A Homo sapiens
3.5.1.14 38.3
-
 Nalpha-acetylmethionine pH 7.4, 22°C, recombinant wild-type enzyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.14 7.4
-
 assay at Homo sapiens