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Literature summary extracted from

  • Park, S.H.; Lee, C.W.; Lee, S.G.; Shin, S.C.; Kim, H.J.; Park, H.; Lee, J.H.
    Crystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H (2017), PLoS ONE, 12, e0181705 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.19.5 expression in Escherichia coli BL21 (DE3) Colwellia psychrerythraea

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.19.5 structures of the isoaspartyl dipeptidase from Colwellia psychrerythraea, both ligand-free and that complexed with beta-isoaspartyl lysine, at 1.85 A and 2.33 A resolution, respectively. In both structures, the enzyme forms an octamer with two Zn2+ ions in the active site Colwellia psychrerythraea

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.5 E166A the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature Colwellia psychrerythraea
3.4.19.5 E166K the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature Colwellia psychrerythraea
3.4.19.5 E80Q the mutant has no catalytic activity toward beta-Asp-Leu, but its CD spectra and denaturation temperature are similar to wild-type, indicating that this mutation affects catalytic activity but not the overall folding and integrity of the enzyme Colwellia psychrerythraea
3.4.19.5 Y140F the mutant has a significant reduction rate of catalysis confirming that this tyrosine residue is important for enzymatic catalysis. It shows less than 10% catalytic activity toward beta-Asp-Leu and the CD spectrum is not significantly different to the wild-type enzyme. Unlike the wild-type enzyme and the other mutants Y140F has a tendency to aggregate during purification and storage, but soluble Y140F is the most thermally stable Colwellia psychrerythraea

General Stability

EC Number General Stability Organism
3.4.19.5 thermostable, probably owing to its octameric structure Colwellia psychrerythraea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.5 0.49
-
 beta-Asp-Phe pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 0.71
-
 beta-Asp-Leu pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 0.93
-
 beta-Ala-Ala pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 1.1
-
 beta-Asp-Lys pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 1.2
-
 beta-Asp-Ala pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 4.7
-
 beta-Asp-Gly pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 5.3
-
 beta-Asp-His pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 6.9
-
 alpha-Asp-Leu pH 8.0, 30°C Colwellia psychrerythraea

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.5 Colwellia psychrerythraea Q484B6
-
-
3.4.19.5 Colwellia psychrerythraea ATCC BAA-681 Q484B6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.5
-
 Colwellia psychrerythraea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.5 alpha-Asp-Leu + H2O
-
 Colwellia psychrerythraea Asp + Leu
-
 ?
3.4.19.5 beta-Ala-Ala + H2O
-
 Colwellia psychrerythraea Ala + Ala
-
 ?
3.4.19.5 beta-Asp-Ala + H2O
-
 Colwellia psychrerythraea Asp + Ala
-
 ?
3.4.19.5 beta-Asp-Ala + H2O
-
 Colwellia psychrerythraea ATCC BAA-681 Asp + Ala
-
 ?
3.4.19.5 beta-Asp-Gly + H2O
-
 Colwellia psychrerythraea Asp + Gly
-
 ?
3.4.19.5 beta-Asp-Gly + H2O
-
 Colwellia psychrerythraea ATCC BAA-681 Asp + Gly
-
 ?
3.4.19.5 beta-Asp-His + H2O
-
 Colwellia psychrerythraea Asp + His
-
 ?
3.4.19.5 beta-Asp-His + H2O
-
 Colwellia psychrerythraea ATCC BAA-681 Asp + His
-
 ?
3.4.19.5 beta-Asp-Leu + H2O
-
 Colwellia psychrerythraea Asp + Leu
-
 ?
3.4.19.5 beta-Asp-Leu + H2O
-
 Colwellia psychrerythraea ATCC BAA-681 Asp + Leu
-
 ?
3.4.19.5 beta-Asp-Lys + H2O
-
 Colwellia psychrerythraea Asp + Lys
-
 ?
3.4.19.5 beta-Asp-Lys + H2O
-
 Colwellia psychrerythraea ATCC BAA-681 Asp + Lys
-
 ?
3.4.19.5 beta-Asp-Phe + H2O
-
 Colwellia psychrerythraea Asp + Phe
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.19.5 octamer crystallographic data, the enzyme forms an octamer with two Zn2+ ions in the active site Colwellia psychrerythraea

Synonyms

EC Number Synonyms Comment Organism
3.4.19.5 CpsIadA
-
 Colwellia psychrerythraea
3.4.19.5 isoaspartyl aminopeptidase/asparaginase
-
 Colwellia psychrerythraea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.19.5 45
-
-
 Colwellia psychrerythraea

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.19.5 30 50 30°C: about 60% of maximal activity, 50°C: about 70% of maximal activity Colwellia psychrerythraea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.19.5 60
-
 completely inactivated Colwellia psychrerythraea
3.4.19.5 66
-
 denaturation temperature, mutant enzyme E166K Colwellia psychrerythraea
3.4.19.5 71
-
 denaturation temperature, mutant enzyme E166A Colwellia psychrerythraea
3.4.19.5 81
-
 denaturation temperature, wild-type enzyme Colwellia psychrerythraea
3.4.19.5 85
-
 denaturation temperature, mutant enzyme E80Q Colwellia psychrerythraea
3.4.19.5 89
-
 denaturation temperature, mutant enzyme Y140F Colwellia psychrerythraea

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.19.5 74
-
 beta-Asp-His pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 89
-
 alpha-Asp-Leu pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 145
-
 beta-Asp-Phe pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 164
-
 beta-Asp-Leu pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 166
-
 beta-Asp-Ala pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 181
-
 beta-Asp-Gly pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 256
-
 beta-Asp-Lys pH 8.0, 30°C Colwellia psychrerythraea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.5 8 8.5
-
 Colwellia psychrerythraea

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.19.5 7.5 9 pH 7.5: about 35% of maximal activity, pH 9.0: about 20% of maximal activity Colwellia psychrerythraea

General Information

EC Number General Information Comment Organism
3.4.19.5 additional information the enzyme catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the beta-carboxyl group side chain of Asp and the amino group of the following amino acid Colwellia psychrerythraea

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.19.5 13
-
 alpha-Asp-Leu pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 14
-
 beta-Asp-His pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 38
-
 beta-Asp-Gly pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 140
-
 beta-Asp-Ala pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 230
-
 beta-Asp-Lys pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 230.9
-
 beta-Asp-Leu pH 8.0, 30°C Colwellia psychrerythraea
3.4.19.5 300
-
 beta-Asp-Phe pH 8.0, 30°C Colwellia psychrerythraea