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Literature summary for 3.4.19.5 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
Search for more literature for 3.4.19.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Escherichia coli P39377
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
IAD
-
 Escherichia coli
isoaspartyl dipeptidase
-
 Escherichia coli

Turnover Number [1/s]

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