2.3.2.20: cyclo(L-leucyl-L-phenylalanyl) synthase
This is an abbreviated version!
For detailed information about cyclo(L-leucyl-L-phenylalanyl) synthase, go to the full flat file.
Word Map on EC 2.3.2.20
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2.3.2.20
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cdpss
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diketopiperazine
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synthetases
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aminoacylated
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2,5-diketopiperazines
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nonribosomal
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trna-dependent
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prenyltransferase
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aa-trnas
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aarss
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class-i
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nocardiopsis
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prenylation
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hijack
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bond-forming
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ping-pong
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synthesis
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tryptophan-containing
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synthetase-like
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noursei
- 2.3.2.20
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cdpss
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diketopiperazine
- synthetases
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aminoacylated
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2,5-diketopiperazines
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nonribosomal
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trna-dependent
- prenyltransferase
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aa-trnas
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aarss
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class-i
- nocardiopsis
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prenylation
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hijack
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bond-forming
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ping-pong
- synthesis
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tryptophan-containing
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synthetase-like
- noursei
Reaction
Synonyms
AlbC, BcmA, CDP, CDPS, CDPS 22, CDPS39, cFL synthase, cyclodipeptide synthase, cyclodipeptide synthases, Fdum-CDPS, Nbra-CDPS, NcdA, NCTC11370_02388, Ndas_1148, NozA, O3I_025450, Rgry-CDPS, RICGR_0139
ECTree
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Substrates Products
Substrates Products on EC 2.3.2.20 - cyclo(L-leucyl-L-phenylalanyl) synthase
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REACTION DIAGRAM
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
L-phenylalanyl-tRNAPhe + L-leucyl-tRNALeu
tRNAPhe + tRNALeu + cyclo(L-phenylalanyl-L-leucyl)
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?
L-phenylalanyl-tRNAPhe + L-methionyl-tRNAMet
tRNAPhe + tRNAMet + cyclo(L-phenylalanyl-L-methionyl)
L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
L-phenylalanyl-tRNAPhe + L-prolyl-tRNAPro
tRNAPhe + tRNAPro + cyclo(L-phenylalanyl-L-prolyl)
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?
L-phenylalanyl-tRNAPhe + L-tyrosinyl-tRNATyr
tRNAPhe + tRNATyr + cyclo(L-phenylalanyl-L-tyrosinyl)
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?
L-tryptophanyl-tRNATrp + L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
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?
L-tyrosinyl-tRNATyr + L-prolyl-tRNAPro
tRNATyr + tRNAPro + cyclo(L-tyrosinyl-L-prolyl)
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?
L-tyrosinyl-tRNATyr + L-valyl-tRNAVal
tRNATyr + tRNAVal + cyclo(L-tyrosinyl-L-valyl)
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?
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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second best activity
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?
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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second best activity
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?
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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highest activity
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?
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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?
L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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intermediate product of the biosynthetic pathway to albonoursin, cyclo(alpha,beta-dehydroPhe-alpha,beta-dehydroLeu)
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L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe
tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl)
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the enzyme uses more efficiently Phe-tRNAPhe than any of the Leu-tRNALeu. The efficiency of cyclo(L-phenylalanyl-L-phenylalanyl) synthesis is not affected by the presence of Leu-tRNALeuGAG or Leu-tRNALeuTAA indicating that these molecules do not compete with Phe-tRNAPhe for binding to the enzyme. In contrast, Leu-tRNALeuCAA, Leu-tRNALeuTAG or or Leu-tRNALeuCAG isoacceptors inhibit cyclo(L-phenylalanyl-L-phenylalanyl) synthesis revealing a competition with Phe-tRNAPhe
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tRNAPhe + tRNAMet + cyclo(L-phenylalanyl-L-methionyl)
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lowest activity
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?
L-phenylalanyl-tRNAPhe + L-methionyl-tRNAMet
tRNAPhe + tRNAMet + cyclo(L-phenylalanyl-L-methionyl)
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lowest activity
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?
L-phenylalanyl-tRNAPhe + L-methionyl-tRNAMet
tRNAPhe + tRNAMet + cyclo(L-phenylalanyl-L-methionyl)
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lowest activity
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?
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
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highest activity
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?
L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
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highest activity
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?
L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
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second best activity
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?
L-phenylalanyl-tRNAPhe + L-phenylalanyl-tRNAPhe
2 tRNAPhe + cyclo(L-phenylalanyl-L-phenylalanyl)
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?
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cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides
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additional information
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cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides
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additional information
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cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides
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additional information
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the enzyme does not accept other aromatic aminoacyl-tRNA substrates than L-tryptophanyl-tRNA
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additional information
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cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides
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additional information
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Rickettsiella grylli ATCC 700358
cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides
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additional information
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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
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additional information
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enzyme AlbC uses aminoacyl-tRNAs to synthesize various cyclodipeptides, including the reactions of cyclo(L-tyrosyl-L-tyrosyl) synthase, EC 2.3.2.21, and cyclo(L-leucyl-L-leucyl) synthase, EC 2.3.2.22
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additional information
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enzyme AlbC uses aminoacyl-tRNAs to synthesize various cyclodipeptides, including the reactions of cyclo(L-tyrosyl-L-tyrosyl) synthase, EC 2.3.2.21, and cyclo(L-leucyl-L-leucyl) synthase, EC 2.3.2.22
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additional information
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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
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additional information
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cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides
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additional information
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mechanism of cyclization with the participation of Y202 in the catalytic function, roles of important residues E182, Y178, N40, and H203, detailed overview
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additional information
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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
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