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Literature summary extracted from

  • Marti-Arbona, R.; Fresquet, V.; Thoden, J.B.; Davis, M.L.; Holden, H.M.; Raushel, F.M.
    Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli (2005), Biochemistry, 44, 7115-7124.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.19.5
-
Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.19.5 hanging drop vapor diffusion method. X-ray crystal structure of the D285N mutant complexed with beta-Asp-His Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.5 D285A kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value Escherichia coli
3.4.19.5 D285N kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value Escherichia coli
3.4.19.5 E77D kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value Escherichia coli
3.4.19.5 E77Q kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value Escherichia coli
3.4.19.5 R169K kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value Escherichia coli
3.4.19.5 R169M kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value Escherichia coli
3.4.19.5 R233K kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value Escherichia coli
3.4.19.5 R233M kcat/Km for beta-Asp-Leu is 170fold lower than wild-type value Escherichia coli
3.4.19.5 S289A kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value Escherichia coli
3.4.19.5 Y137A kcat/Km for beta-Asp-Leu is 927fold lower than wild-type value Escherichia coli
3.4.19.5 Y137F kcat/Km for beta-Asp-Leu is 850fold lower than wild-type value Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.5 0.09
-
beta-Asp-Leu Ni/Ni reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.23
-
beta-Asp-Phe wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.36
-
beta-Asp-Leu Cd/Cd reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.5
-
beta-Asp-Leu mutant enzyme D285A, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.62
-
beta-Asp-Leu Co/Co reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.8
-
beta-Asp-Leu mutant enzyme E77Q, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.91
-
beta-Asp-Lys wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.98
-
beta-Asp-Leu mutant enzyme D285N, pH 8.1, 30°C Escherichia coli
3.4.19.5 1.02
-
beta-Asp-Leu wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 1.02
-
beta-Asp-Leu Zn/Zn reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 1.4
-
beta-Asp-Leu mutant enzyme Y137F, pH 8.1, 30°C Escherichia coli
3.4.19.5 1.7
-
beta-Asp-Leu mutant enzyme Y137A, pH 8.1, 30°C Escherichia coli
3.4.19.5 2.7
-
beta-Asp-Leu mutant enzyme S289A, pH 8.1, 30°C Escherichia coli
3.4.19.5 3.7
-
beta-Asp-His wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 3.7
-
beta-Asp-Ala wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 5
-
alpha-Asp-Leu wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 6.9
-
beta-Asp-Leu mutant enzyme E77D, pH 8.1, 30°C Escherichia coli
3.4.19.5 18
-
beta-Asp-Gly wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 20
-
beta-Asp-Leu mutant enzyme R233K, pH 8.1, 30°C Escherichia coli
3.4.19.5 34
-
beta-Asp-Leu mutant enzyme R169K, pH 8.1, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.19.5 additional information the active site consists of a binuclear metal center positioned at the C-terminal end of a (beta/alpha)8-barrel domain Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.5 Escherichia coli P39377
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.5 alpha-Asp-Leu + H2O
-
Escherichia coli L-Asp + L-Leu
-
?
3.4.19.5 beta-Asp-Ala + H2O
-
Escherichia coli Asp + Ala
-
?
3.4.19.5 beta-Asp-Gly + H2O
-
Escherichia coli Asp + Gly
-
?
3.4.19.5 beta-Asp-His + H2O
-
Escherichia coli Asp + His
-
?
3.4.19.5 beta-Asp-Leu + H2O
-
Escherichia coli Asp + Leu
-
?
3.4.19.5 beta-Asp-Lys + H2O
-
Escherichia coli Asp + Lys
-
?
3.4.19.5 beta-Asp-Phe + H2O
-
Escherichia coli Asp + Phe
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.19.5 IAD
-
Escherichia coli
3.4.19.5 isoaspartyl dipeptidase
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.19.5 0.00062
-
beta-Asp-Leu mutant enzyme D285A, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.0051
-
beta-Asp-Leu mutant enzyme E77D, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.0056
-
beta-Asp-Leu mutant enzyme E77Q, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.017
-
beta-Asp-Leu mutant enzyme D285N, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.18
-
beta-Asp-Leu mutant enzyme Y137F, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.19
-
beta-Asp-Leu mutant enzyme Y137A, pH 8.1, 30°C Escherichia coli
3.4.19.5 0.93
-
beta-Asp-Gly wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 9
-
beta-Asp-Leu mutant enzyme R169K, pH 8.1, 30°C Escherichia coli
3.4.19.5 9
-
beta-Asp-Leu mutant enzyme S289A, pH 8.1, 30°C Escherichia coli
3.4.19.5 9.2
-
beta-Asp-Leu Ni/Ni reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 11.9
-
beta-Asp-Leu Cd/Cd reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 13
-
beta-Asp-Leu mutant enzyme R233K, pH 8.1, 30°C Escherichia coli
3.4.19.5 15.7
-
alpha-Asp-Leu wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 16.9
-
beta-Asp-Phe wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 20.8
-
beta-Asp-His wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 34
-
beta-Asp-Leu Co/Co reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 58
-
beta-Asp-Lys wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 104
-
beta-Asp-Leu wild-type enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 104
-
beta-Asp-Leu Zn/Zn reconstituted enzyme, pH 8.1, 30°C Escherichia coli
3.4.19.5 213
-
beta-Asp-Ala wild-type enzyme, pH 8.1, 30°C Escherichia coli