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Literature summary extracted from

  • Canu, N.; Belin, P.; Thai, R.; Correia, I.; Lequin, O.; Seguin, J.; Moutiez, M.; Gondry, M.
    Incorporation of non-canonical amino acids into 2,5-diketopiperazines by cyclodipeptide synthases (2018), Angew. Chem. Int. Ed. Engl., 57, 3118-3122 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.2.20 synthesis CDPSs are good candidates for the biological production of 2,5-diketopiperazines (2,5-DKPs) because their heterologous expression in Escherichia coli is easy to implement and leads up to high amounts of cyclodipeptides recovered in culture supernatants. CDPSs are often found within biosynthetic gene clusters containing diverse tailoring enzymes responsible for further chemical modifications of the produced cyclodipeptides Rickettsiella massiliensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.20 azetidine-2-carboxylic acid Aze, production of cyclo(Tyr-Val) is slightly decreased by the addition of Aze, which may reflect competition of Aze versus Val Rickettsiella massiliensis

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.20 Rickettsiella massiliensis
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.20 L-phenylalanyl-tRNAPhe + L-prolyl-tRNAPro
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 Rickettsiella massiliensis tRNAPhe + tRNAPro + cyclo(L-phenylalanyl-L-prolyl)
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 ?
2.3.2.20 L-tyrosinyl-tRNATyr + L-prolyl-tRNAPro
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 Rickettsiella massiliensis tRNATyr + tRNAPro + cyclo(L-tyrosinyl-L-prolyl)
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 ?
2.3.2.20 L-tyrosinyl-tRNATyr + L-valyl-tRNAVal
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 Rickettsiella massiliensis tRNATyr + tRNAVal + cyclo(L-tyrosinyl-L-valyl)
-
 ?
2.3.2.20 additional information in vivo method for incorporating non-canonical amino acids (ncAAs) into 2,5-DKPs using cyclodipeptide synthases (CDPSs), exploitation of the natural ability of aminoacyl-tRNA synthetases to load ncAAs onto tRNAs, substrate specificity, detailed overview Rickettsiella massiliensis ?
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Synonyms

EC Number Synonyms Comment Organism
2.3.2.20 CDPS
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 Rickettsiella massiliensis
2.3.2.20 CDPS 22
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 Rickettsiella massiliensis
2.3.2.20 cyclodipeptide synthase
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 Rickettsiella massiliensis

General Information

EC Number General Information Comment Organism
2.3.2.20 metabolism various cyclodipeptide-tailoring enzymes are found in 2,5-diketopiperazine (2,5-DKP) biosynthetic pathways Rickettsiella massiliensis
2.3.2.20 additional information the CDPS adopts a common architecture with a monomer built around a Rossmann fold domain that displays structural similarity to the catalytic domain of the two class Ic aminoacyl-tRNA synthetases (aaRSs), TyrRS and TrpRS. It contains a deep surface-accessible pocket P1, the location of which corresponds to that of the aminoacyl-binding pocket of the two aaRSs. Catalytic mechanism, overview Rickettsiella massiliensis
2.3.2.20 physiological function cyclodipeptide synthases incorporate non-canonical amino acids into 2,5-diketopiperazines through a ping-pong catalytic mechanism for the stereospecific formation of various cyclodipeptides [cyclo(l-AA1-l-AA2), with AA1 and AA2 corresponding to the two incorporated aminoacyl moieties] Rickettsiella massiliensis