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Literature summary for 2.3.2.20 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
Search for more literature for 2.3.2.20

Application

Application Comment Organism
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

Inhibitors Comment Organism Structure
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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanyl-tRNAPhe + L-prolyl-tRNAPro
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 Rickettsiella massiliensis tRNAPhe + tRNAPro + cyclo(L-phenylalanyl-L-prolyl)
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 ?
L-tyrosinyl-tRNATyr + L-prolyl-tRNAPro
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 Rickettsiella massiliensis tRNATyr + tRNAPro + cyclo(L-tyrosinyl-L-prolyl)
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 ?
L-tyrosinyl-tRNATyr + L-valyl-tRNAVal
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 Rickettsiella massiliensis tRNATyr + tRNAVal + cyclo(L-tyrosinyl-L-valyl)
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 ?
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

Synonyms Comment Organism
CDPS
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 Rickettsiella massiliensis
CDPS 22
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 Rickettsiella massiliensis
cyclodipeptide synthase
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 Rickettsiella massiliensis

General Information

General Information Comment Organism
metabolism various cyclodipeptide-tailoring enzymes are found in 2,5-diketopiperazine (2,5-DKP) biosynthetic pathways Rickettsiella massiliensis
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
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