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Literature summary for 2.3.2.21 extracted from

  • Borgman, P.; Lopez, R.; Lane, A.
    The expanding spectrum of diketopiperazine natural product biosynthetic pathways containing cyclodipeptide synthases (2019), Org. Biomol. Chem., 17, 2305-2314 .
    View publication on PubMed
Search for more literature for 2.3.2.21

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-tyrosyl-tRNATyr Mycobacterium tuberculosis
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 2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
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 ?
additional information Mycobacterium tuberculosis Rv2275 is established as a CDPS that catalyzes formation of cyclo(L-tyrosyl-L-tyrosyl) as its major product, along with a handful of minor products containing tyrosine ?
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Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WPF9
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-tyrosyl-tRNATyr
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 Mycobacterium tuberculosis 2 tRNATyr + cyclo(L-tyrosyl-L-tyrosyl)
-
 ?
additional information Rv2275 is established as a CDPS that catalyzes formation of cyclo(L-tyrosyl-L-tyrosyl) as its major product, along with a handful of minor products containing tyrosine Mycobacterium tuberculosis ?
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-

Synonyms

Synonyms Comment Organism
CDPS
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 Mycobacterium tuberculosis
cyclodipeptide synthase
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 Mycobacterium tuberculosis
Rv2275
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 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism comparison of different CDPS-containing biosynthetic pathways, enzyme Rv2275 is involved in the mycocyclosin biosynthetic pathway, overview. Rv2275 is established as a CDPS that catalyzes formation of cyclo(L-tyrosyl-L-tyrosyl) as its major product, along with a handful of minor products containing tyrosine Mycobacterium tuberculosis
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 Mycobacterium tuberculosis
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 Mycobacterium tuberculosis