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 .
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 |