The Enzyme Database

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EC 1.14.15.13     
Accepted name: pulcherriminic acid synthase
Reaction: cyclo(L-leucyl-L-leucyl) + 6 reduced ferredoxin + 3 O2 = pulcherriminic acid + 6 oxidized ferredoxin + 4 H2O
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
pulcherriminic acid = 2,5-dihydroxy-3,6-bis(2-methylpropyl)pyrazine bis-N-oxide
Other name(s): cyclo-L-leucyl-L-leucyl dipeptide oxidase; CYP134A1; CypX (ambiguous)
Systematic name: cyclo(L-leucyl-L-leucyl),reduced-ferredoxin:oxygen oxidoreductase (N-hydroxylating,aromatizing)
Comments: A heme-thiolate (P-450) enzyme from the bacterium Bacillus subtilis. The order of events during the overall reaction is unknown. Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  MacDonald, J.C. Biosynthesis of pulcherriminic acid. Biochem. J. 96 (1965) 533–538. [PMID: 5837792]
2.  Cryle, M.J., Bell, S.G. and Schlichting, I. Structural and biochemical characterization of the cytochrome P450 CypX (CYP134A1) from Bacillus subtilis: a cyclo-L-leucyl-L-leucyl dipeptide oxidase. Biochemistry 49 (2010) 7282–7296. [DOI] [PMID: 20690619]
[EC 1.14.15.13 created 2013]
 
 
EC 2.3.2.22     
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
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.  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]
[EC 2.3.2.22 created 2013]
 
 


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