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Literature summary for 2.3.2.20 extracted from
- The expanding spectrum of diketopiperazine natural product biosynthetic pathways containing cyclodipeptide synthases (2019), Org. Biomol. Chem., 17, 2305-2314 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bmcA, recombinant expression of the bcm cluster in heterologous host Streptomyces coelicolor, resulting in production of bicyclomycin | Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanyl-tRNAPhe + L-leucyl-tRNALeu | Streptomyces noursei | - |
tRNAPhe + tRNALeu + cyclo(L-phenylalanyl-L-leucyl) | - |
? |  |
| additional information | Streptomyces noursei | assembly of the cyclo-Phe-Leu precursor of albonoursin is catalyzed by CDPS AlbC, which also yields a variety of other cyclic dipeptides as minor products | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Nocardiopsis dassonvillei | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei CIP 107115 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei DSM 43111 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei IMRU 509 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei JCM 7437 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei KCTC 9190 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei NBRC 14626 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei NCTC 10488 | D7B1W8 | - |
- |
| Nocardiopsis dassonvillei NRRL B-5397 | D7B1W8 | - |
- |
| Pseudomonas aeruginosa | - |
- |
- |
| Streptomyces noursei | Q8GED7 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanyl-tRNAPhe + L-leucyl-tRNALeu | - |
Streptomyces noursei | tRNAPhe + tRNALeu + cyclo(L-phenylalanyl-L-leucyl) | - |
? | |
| additional information | assembly of the cyclo-Phe-Leu precursor of albonoursin is catalyzed by CDPS AlbC, which also yields a variety of other cyclic dipeptides as minor products | Streptomyces noursei | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AlbC | - |
Streptomyces noursei |
| BcmA | - |
Pseudomonas aeruginosa |
| CDPS | - |
Pseudomonas aeruginosa |
| CDPS | - |
Streptomyces noursei |
| CDPS | - |
Nocardiopsis dassonvillei |
| cyclodipeptide synthase | - |
Pseudomonas aeruginosa |
| cyclodipeptide synthase | - |
Streptomyces noursei |
| cyclodipeptide synthase | - |
Nocardiopsis dassonvillei |
| Ndas_1148 | - |
Nocardiopsis dassonvillei |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | methyltransferase homologues are commonly encoded within putative CDPS gene clusters, yet methyltransferases from only two of these clusters have been characterized to date. One leads to methylated members of the nocazine/XR334 (e.g. XR334) family and the other catalyzes DKP N-methylation of cyclo(L-tryptophanyl-L-tryptophanyl) (cWW) to yield dimethyl-cyclo-Trp-Trp (Me2-cWW) | Nocardiopsis dassonvillei |
| metabolism | comparison of different CDPS-containing biosynthetic pathways, enzyme AlbC is involved in the albonoursin biosynthetic pathway, overview. Assembly of the cyclo-Phe-Leu precursor of albonoursin is catalyzed by CDPS AlbC, which also yields a variety of other cyclic dipeptides as minor products | Streptomyces noursei |
| metabolism | comparison of different CDPS-containing biosynthetic pathways, enzyme BcmA is involved in the bicyclomycin biosynthetic pathway, overview. The proposed bicyclomycin (i.e. (1S,6R)-6-hydroxy-5-methylidene-1-[(2S)-1,2,3-trihydroxy-2-methylpropyl]-2-oxa-7,9-diazabicyclo[4.2.2]decane-8,10-dione) biosynthetic pathway features a cascade of oxidative transformations | Pseudomonas aeruginosa |
| metabolism | comparison of different CDPS-containing biosynthetic pathways, the enzyme encoded by gene ndas_1148 is involved in the XR334 (i.e. (3Z,6Z)-3-benzylidene-6-[(4-methoxyphenyl)methylidene]piperazine-2,5-dione) biosynthetic pathway, overview | Nocardiopsis dassonvillei |
| additional information | the CDPS catalytic mechanism entails initial covalent tethering of the aminoacyl moiety from the first aa-tRNA substrate onto a conserved active site serine (Ser) residue. Nucleophilic attack of the amino nitrogen on the carbonyl carbon from the second aa-tRNA substrate yields the first peptide bond. The resulting enzyme-linked dipeptidyl intermediate then undergoes intramolecular peptide bond formation to yield the DKP group with concomitant release from the active site. The two aa-tRNA substrates bind at different sites of the CDPS | Pseudomonas aeruginosa |
| additional information | the CDPS catalytic mechanism entails initial covalent tethering of the aminoacyl moiety from the first aa-tRNA substrate onto a conserved active site serine (Ser) residue. Nucleophilic attack of the amino nitrogen on the carbonyl carbon from the second aa-tRNA substrate yields the first peptide bond. The resulting enzyme-linked dipeptidyl intermediate then undergoes intramolecular peptide bond formation to yield the DKP group with concomitant release from the active site. The two aa-tRNA substrates bind at different sites of the CDPS | Streptomyces noursei |
| additional information | the CDPS catalytic mechanism entails initial covalent tethering of the aminoacyl moiety from the first aa-tRNA substrate onto a conserved active site serine (Ser) residue. Nucleophilic attack of the amino nitrogen on the carbonyl carbon from the second aa-tRNA substrate yields the first peptide bond. The resulting enzyme-linked dipeptidyl intermediate then undergoes intramolecular peptide bond formation to yield the DKP group with concomitant release from the active site. The two aa-tRNA substrates bind at different sites of the CDPS | Nocardiopsis dassonvillei |
| physiological function | cyclodipeptide synthases (CDPSs) are recognized catalysts of 2,5-diketopiperazine (DKP) assembly, employing two aminoacyl-tRNAs (aa-tRNAs) as substrates. Representative 2,5-diketopiperazine (DKP) natural products and bioactivities, overview | Pseudomonas aeruginosa |
| physiological function | cyclodipeptide synthases (CDPSs) are recognized catalysts of 2,5-diketopiperazine (DKP) assembly, employing two aminoacyl-tRNAs (aa-tRNAs) as substrates. Representative 2,5-diketopiperazine (DKP) natural products and bioactivities, overview | Streptomyces noursei |
| physiological function | cyclodipeptide synthases (CDPSs) are recognized catalysts of 2,5-diketopiperazine (DKP) assembly, employing two aminoacyl-tRNAs (aa-tRNAs) as substrates. Representative 2,5-diketopiperazine (DKP) natural products and bioactivities, overview | Nocardiopsis dassonvillei |
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