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Literature summary for 3.5.1.14 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

Protein Variants Comment Organism
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
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
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
H206N site-directed mutagenesis, dimerization domain mutant, the mutant shows 11837fold reduced activity compared to the wild-type enzyme Homo sapiens
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
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
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
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.39
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant D274A Homo sapiens
0.43
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant wild-type enzyme Homo sapiens
0.54
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206A Homo sapiens
0.58
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206K Homo sapiens
0.78
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant N263D Homo sapiens
2.02
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant H206N Homo sapiens
67.4
-
Nalpha-acetylmethionine pH 7.4, 22°C, recombinant mutant R276A Homo sapiens

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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