The Enzyme Database

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Accepted name: cyclo(L-leucyl-L-leucyl) synthase
Reaction: 2 L-leucyl-tRNALeu = 2 tRNALeu + cyclo(L-leucyl-L-leucyl)
For diagram of cyclic dipeptide biosynthesis, click here
Glossary: cyclo(L-leucyl-L-leucyl) = (3S,6S)-3,6-bis(2-methylpropyl)piperazine-2,5-dione
Other name(s): YvmC; cLL synthase; cyclodileucine synthase
Systematic name: L-leucyl-tRNALeu:L-leucyl-tRNALeu leucyltransferase (cyclizing)
Comments: The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the first L-leucine residue [2]. The proteins from bacteria of the genus Bacillus also form small amounts of cyclo(L-phenylalanyl-L-leucyl) and cyclo(L-leucyl-L-methionyl) [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Gondry, M., Sauguet, L., Belin, P., Thai, R., Amouroux, R., Tellier, C., Tuphile, K., Jacquet, M., Braud, S., Courcon, M., Masson, C., Dubois, S., Lautru, S., Lecoq, A., Hashimoto, S., Genet, R. and Pernodet, J.L. Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes. Nat. Chem. Biol. 5 (2009) 414–420. [DOI] [PMID: 19430487]
2.  Bonnefond, L., Arai, T., Sakaguchi, Y., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA synthetase paralog. Proc. Natl. Acad. Sci. USA 108 (2011) 3912–3917. [DOI] [PMID: 21325056]
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