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Literature summary for 4.3.2.8 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)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

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

Protein Variants

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BVM4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
epsilon-(gamma-L-glutamyl)-L-lysine
-
Homo sapiens L-lysine + 5-oxo-L-proline
-
?
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

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