Reaction participants Show >> << Hide
- Name help_outline ε-(γ-L-glutamyl)-L-lysine Identifier CHEBI:133752 Charge 0 Formula C11H21N3O5 InChIKeyhelp_outline JPKNLFVGUZRHOB-YUMQZZPRSA-N SMILEShelp_outline O=C(CC[C@H]([NH3+])C([O-])=O)NCCCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-oxo-L-proline Identifier CHEBI:58402 (Beilstein: 4783230) help_outline Charge -1 Formula C5H6NO3 InChIKeyhelp_outline ODHCTXKNWHHXJC-VKHMYHEASA-M SMILEShelp_outline [O-]C(=O)[C@@H]1CCC(=O)N1 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-lysine Identifier CHEBI:32551 Charge 1 Formula C6H15N2O2 InChIKeyhelp_outline KDXKERNSBIXSRK-YFKPBYRVSA-O SMILEShelp_outline [NH3+]CCCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 65 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:16961 | RHEA:16962 | RHEA:16963 | RHEA:16964 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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gamma-Glutamylamine cyclotransferase: specificity toward epsilon-(L-gamma-glutamyl)-L-lysine and related compounds.
Fink M.L., Chung S.I., Folk J.E.
gamma-Glutamylamine cyclotransferase, an enzyme that catalyzes the conversion of L-gamma-glutamylamines to free amines and 5-oxo-L-proline, was found in rabbit kidney and in various other tissues. The specificity of this enzyme indicates that it functions in the metabolism of products of transglut ... >> More
gamma-Glutamylamine cyclotransferase, an enzyme that catalyzes the conversion of L-gamma-glutamylamines to free amines and 5-oxo-L-proline, was found in rabbit kidney and in various other tissues. The specificity of this enzyme indicates that it functions in the metabolism of products of transglutaminase action; among its substrates are epsilon-(L-gamma-glutamyl)-L-lysine, a derivative of this peptide in which the alpha-amino and carboxyl groups of the lysine moiety are blocked, and L-gamma-glutamyl-polyamine derivatives. << Less
Proc Natl Acad Sci U S A 77:4564-4568(1980) [PubMed] [EuropePMC]
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Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism.
Oakley A.J., Coggan M., Board P.G.
Gamma-glutamylamine cyclotransferase (GGACT) is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts ... >> More
Gamma-glutamylamine cyclotransferase (GGACT) is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase (GGCT), an enzyme with activity toward gamma-glutamyl-alpha-amino acids (Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., and Board, P. G. (2008) J. Biol. Chem. 283, 22031-22042). Despite the absence of significant sequence identity, several residues are conserved in the active sites of GGCT and GGACT, including a putative catalytic acid/base residue (GGACT Glu(82)). The structure of GGACT in complex with the reaction product 5-oxoproline provides evidence for a common catalytic mechanism in both enzymes. The proposed mechanism, combined with the three-dimensional structures, also explains the different substrate specificities of these enzymes. Despite significant sequence divergence, there are at least three subfamilies in prokaryotes and eukaryotes that have conserved the GGCT fold and GGCT enzymatic activity. << Less