EC 2.3.2.22 - Cyclo(L-leucyl-L-leucyl) synthase

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IntEnz Enzyme Nomenclature
EC 2.3.2.22

Names

Accepted name:
cyclo(L-leucyl-L-leucyl) synthase
Other names:
YvmC
cLL synthase
cyclodileucine synthase
Systematic name:
L-leucyl-tRNALeu:L-leucyl-tRNALeu leucyltransferase (cyclizing)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  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., Pernodet, J. L.
    Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes.
    Nat. Chem. Biol. 5 : 414-420 (2009). [PMID: 19430487]
  2. Bonnefond, L., Arai, T., Sakaguchi, Y., Suzuki, T., Ishitani, R., Nureki, O.
    Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA synthetase paralog.
    Proc. Natl. Acad. Sci. U.S.A. 108 : 3912-3917 (2011). [PMID: 21325056]

[EC 2.3.2.22 created 2013]