The Enzyme Database

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EC 1.3.3.13     
Accepted name: albonoursin synthase
Reaction: cyclo(L-leucyl-L-phenylalanyl) + 2 O2 = albonoursin + 2 H2O2 (overall reaction)
(1a) cyclo(L-leucyl-L-phenylalanyl) + O2 = cyclo[(Z)-α,β-didehydrophenylalanyl-L-leucyl] + H2O2
(1b) cyclo[(Z)-α,β-didehydrophenylalanyl-L-leucyl] + O2 = albonoursin + H2O2
For diagram of cyclic dipeptide biosynthesis, click here
Glossary: cyclo(L-leucyl-L-phenylalanyl) = (3S,6S)-3-benzyl-6-(2-methylpropyl)piperazine-2,5-dione
cyclo[(Z)-α,β-didehydrophenylalanyl-L-leucyl] = (3Z,6S)-3-benzylidene-6-(2-methylpropyl)piperazine-2,5-dione
albonoursin = (3Z,6Z)-3-benzylidene-6-(2-methylpropylidene)piperazine-2,5-dione
Other name(s): cyclo(dipeptide):oxygen oxidoreductase; cyclic dipeptide oxidase; AlbA
Systematic name: cyclo(L-leucyl-L-phenylalanyl):oxygen oxidoreductase
Comments: A flavoprotein from the bacterium Streptomyces noursei. The enzyme can also oxidize several other cyclo dipeptides, the best being cyclo(L-tryptophyl-L-tryptophyl) and cyclo(L-phenylalanyl-L-phenylalanyl) [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gondry, M., Lautru, S., Fusai, G., Meunier, G., Menez, A. and Genet, R. Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl α,β-dehydrogenase. Eur. J. Biochem. 268 (2001) 1712–1721. [DOI] [PMID: 11248691]
2.  Lautru, S., Gondry, M., Genet, R. and Pernodet, J.L. The albonoursin gene cluster of S. noursei. Biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases. Chem. Biol. 9 (2002) 1355–1364. [DOI] [PMID: 12498889]
[EC 1.3.3.13 created 2013]
 
 
EC 2.3.2.20     
Accepted name: cyclo(L-leucyl-L-phenylalanyl) synthase
Reaction: L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe = tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
For diagram of cyclic dipeptide biosynthesis, click here
Glossary: cyclo(L-leucyl-L-phenylalanyl) = (3S,6S)-3-benzyl-6-(2-methylpropyl)piperazine-2,5-dione
Other name(s): AlbC; cFL synthase
Systematic name: L-leucyl-tRNALeu:L-phenylalanyl-tRNAPhe leucyltransferase (cyclizing)
Comments: The reaction proceeds following a ping-pong mechanism forming a covalent intermediate between an active site serine and the L-phenylalanine residue [2]. The protein, found in the bacterium Streptomyces noursei, also forms cyclo(L-phenylalanyl-L-phenylalanyl), cyclo(L-methionyl-L-phenylalanyl), cyclo(L-phenylalanyl-L-tyrosyl) and cyclo(L-methionyl-L-tyrosyl) [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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. 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.  Sauguet, L., Moutiez, M., Li, Y., Belin, P., Seguin, J., Le Du, M.H., Thai, R., Masson, C., Fonvielle, M., Pernodet, J.L., Charbonnier, J.B. and Gondry, M. Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis. Nucleic Acids Res. 39 (2011) 4475–4489. [DOI] [PMID: 21296757]
[EC 2.3.2.20 created 2013]
 
 


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