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Information on EC 4.3.2.8 - gamma-glutamylamine cyclotransferase and Organism(s) Homo sapiens and UniProt Accession Q9BVM4

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.8 gamma-glutamylamine cyclotransferase
IUBMB Comments
The enzyme, found in vertebrates, has no activity toward alpha-(gamma-L-glutamyl)-L-amino acids (cf. EC 4.3.2.9, gamma-glutamylcyclotransferase). The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the gamma-L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline.
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This record set is specific for:
Homo sapiens
UNIPROT: Q9BVM4
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
gamma-glutamylamine cyclotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GGACT
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
epsilon-(gamma-L-glutamyl)-L-lysine gamma-glutamyl cyclotransferase (5-oxo-L-proline producing)
The enzyme, found in vertebrates, has no activity toward alpha-(gamma-L-glutamyl)-L-amino acids (cf. EC 4.3.2.9, gamma-glutamylcyclotransferase). The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the gamma-L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
epsilon-(gamma-L-glutamyl)-L-lysine
L-lysine + 5-oxo-L-proline
show the reaction diagram
-
-
-
?
additional information
?
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no substrates: L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GGACT_HUMAN
153
0
17329
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
gel fitlration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 17327, calculated, 1 * 17300, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of GGACT in complex with the reaction product 5-oxoproline
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E82Q
no catalytic activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oakley, A.J.; Coggan, M.; Board, P.G.
Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism
J. Biol. Chem.
285
9642-9648
2010
Homo sapiens (Q9BVM4)
Manually annotated by BRENDA team