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Literature summary for 3.4.19.5 extracted from

  • Gary, J.D.; Clarke, S.
    Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli (1995), J. Biol. Chem., 270, 4076-4087.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.8
-
beta-aspartyl-L-leucine
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Escherichia coli 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli does not appear to be involved in glutathione metabolism ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-Asp-Leu + H2O
-
Escherichia coli Asp + Leu
-
?
additional information little or no activity towards L-isoaspartyl-glycine or L-isoaspartyl-L-histidine, gamma-L-glutamyl-L-leucine, gamma-L-glutamyl-glycine, gamma-L-glutamyl-L-cysteine, gamma-L-glutamyl-L-histidine Escherichia coli ?
-
?
additional information does not appear to be involved in glutathione metabolism Escherichia coli ?
-
?