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Literature summary for 2.3.2.20 extracted from

  • Moutiez, M.; Seguin, J.; Fonvielle, M.; Belin, P.; Jacques, I.B.; Favry, E.; Arthur, M.; Gondry, M.
    Specificity determinants for the two tRNA substrates of the cyclodipeptide synthase AlbC from Streptomyces noursei (2014), Nucleic Acids Res., 42, 7247-7258.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe Streptomyces noursei the enzyme uses more efficiently Phe-tRNAPhe than any of the Leu-tRNALeu. The efficiency of cyclo(L-phenylalanyl-L-phenylalanyl) synthesis is not affected by the presence of Leu-tRNALeuGAG or Leu-tRNALeuTAA indicating that these molecules do not compete with Phe-tRNAPhe for binding to the enzyme. In contrast, Leu-tRNALeuCAA, Leu-tRNALeuTAG or or Leu-tRNALeuCAG isoacceptors inhibit cyclo(L-phenylalanyl-L-phenylalanyl) synthesis revealing a competition with Phe-tRNAPhe tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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Organism

Organism UniProt Comment Textmining
Streptomyces noursei
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe the enzyme uses more efficiently Phe-tRNAPhe than any of the Leu-tRNALeu. The efficiency of cyclo(L-phenylalanyl-L-phenylalanyl) synthesis is not affected by the presence of Leu-tRNALeuGAG or Leu-tRNALeuTAA indicating that these molecules do not compete with Phe-tRNAPhe for binding to the enzyme. In contrast, Leu-tRNALeuCAA, Leu-tRNALeuTAG or or Leu-tRNALeuCAG isoacceptors inhibit cyclo(L-phenylalanyl-L-phenylalanyl) synthesis revealing a competition with Phe-tRNAPhe Streptomyces noursei tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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Synonyms

Synonyms Comment Organism
AlbC
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Streptomyces noursei
CDPS
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Streptomyces noursei
cyclodipeptide synthase
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Streptomyces noursei