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Literature summary extracted from

  • Oakley, A.J.; Coggan, M.; Board, P.G.
    Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism (2010), J. Biol. Chem., 285, 9642-9648 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.2.8 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.2.8 structure of GGACT in complex with the reaction product 5-oxoproline Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.8 E82A no catalytic activity Homo sapiens
4.3.2.8 E82A enzyme is unstable and readily precipitates Homo sapiens
4.3.2.8 E82Q no catalytic activity Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.2.8 18000
-
 gel fitlration Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.8 Homo sapiens Q9BVM4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.8 epsilon-(gamma-L-glutamyl)-L-lysine
-
 Homo sapiens L-lysine + 5-oxo-L-proline
-
 ?
4.3.2.8 additional information no substrates: L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.2.8 monomer 1 * 17327, calculated, 1 * 17300, SDS-PAGE Homo sapiens