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Literature summary for 2.3.2.20 extracted from

  • Skinnider, M.A.; Johnston, C.W.; Merwin, N.J.; Dejong, C.A.; Magarvey, N.A.
    Global analysis of prokaryotic tRNA-derived cyclodipeptide biosynthesis (2018), BMC Genomics, 19, 45 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.20

Cloned(Commentary)

Cloned (Comment) Organism
gene albC, sequence comparisons and phylogenetic analysis, recombinant expression of codon-optimized gene in Escherichia coli strain M15 Streptomyces noursei

Organism

Organism UniProt Comment Textmining
Streptomyces noursei Q8GED7
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the AlbC catalytic cycle begins with the binding of the first aa-tRNA, with its aminoacyl moiety accommodated in a surface-accessible pocket P1 and transferred onto a conserved serine residue to form an aminoacyl-enzyme intermediate. The second aa-tRNA interacts with this intermediate so that its aminoacyl moiety, accommodated in a wide cavity P2, is transferred to the aminoacyl-enzyme to form a dipeptidyl-enzyme intermediate. Finally, the dipeptidyl moiety undergoes an intramolecular cyclization leading to the final cyclodipeptide Streptomyces noursei ?
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Synonyms

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

General Information

General Information Comment Organism
additional information structural studies on the CDPS AlbChave lead to the identification of the two pockets P1 and P2 and show that these pockets are bordered by eight and seven residues, respectively. Cyclodipeptides produced by CDPSs, general overview Streptomyces noursei