Loading the page.
Proteins/UNIPROT:Q9BVM4
Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine..
Function from UniProtKB (Q9BVM4), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
10 statements
10 statements · 4 reference databases · Subject: GGACT · Sources: Bgee, Hetionet, Human-GEM, Rhea
5 reactions
gamma-L-glutamyl-L-cysteineCHEBI:18183+L-cysteine
Reaction pageLeft to rightBalancedEC 4.3.2.9cytosol
Human-GEM MAR04708CC BY 4.0Reference data
gamma-Glu-AlaCHEBI:18183+L-alanine
Reaction pageLeft to rightBalancedEC 4.3.2.9extracellular space, cytosol
3 names
Resolves to: GGACT
epsilon-(gamma-L-glutamyl)-L-lysineCHEBI:18183+CHEBI:18019
Catalysed by GGACT
Reaction pageLeft to rightBalancedEC 4.3.2.8cytosol
Human-GEM MAR20071CC BY 4.0Reference data
epsilon-(gamma-L-glutamyl)-L-lysineCHEBI:18183+CHEBI:18019
Catalysed by GGACT
Reaction pageLeft to rightBalancedEC 4.3.2.8nucleus
Human-GEM MAR20072CC BY 4.0Reference data
epsilon-(gamma-L-glutamyl)-L-lysine5-oxo-L-proline+L-lysine
Catalysed by GGACT
Reaction pageDirection not assertedBalanced
Rhea RHEA:16961CC BY 4.0Reference data