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Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism

Journal Article


Abstract


  • γ-Glutamylamine cyclotransferase (GGACT) is an enzyme that converts γ-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward γ-glutamyl-ϵ-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in γ-glutamylcyclotransferase (GGCT), an enzyme with activity toward γ-glutamyl-α-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 Glu82). 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.

Authors


  •   Oakley, Aaron J.
  •   Coggan, Marjorie (external author)
  •   Board, Philip G. (external author)

Publication Date


  • 2010

Citation


  • Oakley, A. J., Coggan, M. & Board, P. G. (2010). Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism. Journal of Biological Chemistry, 285 (13), 9642-9648.

Scopus Eid


  • 2-s2.0-77951218927

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/5179

Number Of Pages


  • 6

Start Page


  • 9642

End Page


  • 9648

Volume


  • 285

Issue


  • 13

Place Of Publication


  • http://www.jbc.org/

Abstract


  • γ-Glutamylamine cyclotransferase (GGACT) is an enzyme that converts γ-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward γ-glutamyl-ϵ-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in γ-glutamylcyclotransferase (GGCT), an enzyme with activity toward γ-glutamyl-α-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 Glu82). 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.

Authors


  •   Oakley, Aaron J.
  •   Coggan, Marjorie (external author)
  •   Board, Philip G. (external author)

Publication Date


  • 2010

Citation


  • Oakley, A. J., Coggan, M. & Board, P. G. (2010). Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism. Journal of Biological Chemistry, 285 (13), 9642-9648.

Scopus Eid


  • 2-s2.0-77951218927

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/5179

Number Of Pages


  • 6

Start Page


  • 9642

End Page


  • 9648

Volume


  • 285

Issue


  • 13

Place Of Publication


  • http://www.jbc.org/