| EC |
4.3.2.9 |
| Accepted name: |
γ-glutamylcyclotransferase |
| Reaction: |
α-(γ-L-glutamyl)-L-amino acid = α-L-amino acid + 5-oxo-L-proline |
| Other name(s): |
γ-glutamyl-amino acid cyclotransferase; γ-L-glutamylcyclotransferase; L-glutamic cyclase; (5-L-glutamyl)-L-amino-acid 5-glutamyltransferase (cyclizing); GGCT |
| Systematic name: |
α-(γ-L-glutamyl)-L-amino-acid γ-glutamyl cyclotransferase (5-oxo-L-proline producing) |
| Comments: |
The enzyme, found in animals and plants, acts on derivatives of L-glutamate, L-2-aminobutanoate, L-alanine and glycine. The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the α-amine of the L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-44-7 |
| References: |
| 1. |
Bodnaryk, R.P. and McGirr, L. Purification, properties and function of a unique γ-glutamyl cyclotransferase from the housefly, Musca domestica L. Biochim. Biophys. Acta 315 (1973) 352–362. |
| 2. |
Orlowski, M., Richman, P.G. and Meister, A. Isolation and properties of γ-L-glutamylcyclotransferase from human brain. Biochemistry 8 (1969) 1048–1055. [PMID: 5781001] |
| 3. |
Oakley, A.J., Yamada, T., Liu, D., Coggan, M., Clark, A.G. and Board, P.G. The identification and structural characterization of C7orf24 as γ-glutamyl cyclotransferase. An essential enzyme in the γ-glutamyl cycle. J. Biol. Chem. 283 (2008) 22031–22042. [DOI] [PMID: 18515354] |
| 4. |
Paulose, B., Chhikara, S., Coomey, J., Jung, H.I., Vatamaniuk, O. and Dhankher, O.P. A γ-glutamyl cyclotransferase protects Arabidopsis plants from heavy metal toxicity by recycling glutamate to maintain glutathione homeostasis. Plant Cell 25 (2013) 4580–4595. [DOI] [PMID: 24214398] |
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| [EC 4.3.2.9 created 1972 as EC 2.3.2.4, transferred 2017 to EC 4.3.2.9] |
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