2.3.2.B16: cyclo-(L-Trp-L-Trp) synthase
This is an abbreviated version!
For detailed information about cyclo-(L-Trp-L-Trp) synthase, go to the full flat file.
Word Map on EC 2.3.2.B16
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2.3.2.B16
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archaeological
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highlands
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peruvian
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pre-columbian
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bioarchaeological
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andean
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diachronic
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anthropol
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crania
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ritual
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artist
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hemivertebrae
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mummy
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osteological
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mummified
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professionalism
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radiocarbon
- 2.3.2.B16
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archaeological
-
highlands
-
peruvian
-
pre-columbian
-
bioarchaeological
-
andean
-
diachronic
-
anthropol
-
crania
-
ritual
-
artist
-
hemivertebrae
-
mummy
-
osteological
-
mummified
-
professionalism
-
radiocarbon
Reaction
Synonyms
amir_4627, CDPS, CWPS1NS1868, CWWS1D46488, CWWS1NB2774, CWWS1NB5414, CWWS1NB5737, CWWS2D46488, cyclo-(L-Trp-L-Leu) synthase, cyclo-(L-Trp-L-Pro) synthase, cyclo-(L-Trp-L-Trp) synthase, cyclodipeptide synthase, DmtB, dmtB1, NascA, NcdA, NozA
ECTree
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General Information
General Information on EC 2.3.2.B16 - cyclo-(L-Trp-L-Trp) synthase
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evolution
metabolism
physiological function
additional information
genome sequences from three Streptomyces strains share a homologous locus predicted to encode a CDPS (DmtB), membrane-associated terpene cyclase (DmtA), and phytoene synthase (DmtC)
evolution
methyltransferase homologues are commonly encoded within putative CDPS gene clusters,47 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)
evolution
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
evolution
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
evolution
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
evolution
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
evolution
-
methyltransferase homologues are commonly encoded within putative CDPS gene clusters,47 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)
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evolution
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
evolution
-
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
evolution
-
methyltransferase homologues are commonly encoded within putative CDPS gene clusters,47 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)
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evolution
Streptomyces lavendulae NRRL B-2774
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
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evolution
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
evolution
-
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
evolution
-
methyltransferase homologues are commonly encoded within putative CDPS gene clusters,47 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)
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evolution
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methyltransferase homologues are commonly encoded within putative CDPS gene clusters,47 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)
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evolution
Streptomyces purpureus NRRL B-5737
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
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evolution
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phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
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comparison of different CDPS-containing biosynthetic pathways, enzyme DmtB is involved in the drimentine G (i.e. (3S,5aS,10bS,11aS)-3-(propan-2-yl)-10b-[[(8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-6,10b,11,11a-tetrahydro-2H-pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-1,4(3H,5aH)-dione) biosynthetic pathway, overview
metabolism
comparison of different CDPS-containing biosynthetic pathways, the enzyme encoded by amir_4627 is involved in the dimethyl-cyclo-Trp-Trp (cWW) (Me2-cWW) biosynthetic pathway, it possesses an additional intrinsic methyltransferase activity, overview
metabolism
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comparison of different CDPS-containing biosynthetic pathways, the enzyme is involved in the 1-(8-guaninyl)-cyclic-Trp-Trp (i.e. 1-(8-guaninyl)-cWW or (3S,6S)-3-[[1-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-2,3-dihydro-1H-indol-3-yl]methyl]-6-[(1H-indol-3-yl)methyl]piperazine-2,5-dione) biosynthetic pathway, overview
metabolism
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comparison of nine different CDPS-containing biosynthetic pathways, enzyme NascA is involved in the naseseazine C biosynthetic pathway, overview. Unlike fungal biosynthetic pathways that utilize NRPSs to form DKP precursors of dimeric DKPs, biogenesis of naseseazine C from a marine-derived Streptomyces sp. is linked to a CDPS-containing gene cluster, nascA-nascB, via heterologous expression of this pathway in Streptomyces albus. Sequence homology to characterized CDPSs implicated NascA in assembly of the cyclo(L-tryptophanyl-L-prolyl) (cWP) precursor of naseseazine C, while functional characterization of purified recombinant NascB establishes it as the cytochrome P450 catalyst of intermolecular C-C bond formation between two cWP precursors
metabolism
two distinct cyclodipeptide synthases from a marine actinomycete catalyze biosynthesis of the same diketopiperazine natural product. NozA and NcdA catalyze cyclo(L-Trp-L-Trp) biosynthesis from tryptophanyl-tRNA and do not accept other aromatic aminoacyl-tRNA substrates. Cyclo(L-Trp-L-Trp) is a biosynthetic precursor of the nocardioazines, Nocardiopsis sp. may derive this precursor from both NozA and NcdA
metabolism
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comparison of different CDPS-containing biosynthetic pathways, the enzyme encoded by amir_4627 is involved in the dimethyl-cyclo-Trp-Trp (cWW) (Me2-cWW) biosynthetic pathway, it possesses an additional intrinsic methyltransferase activity, overview
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metabolism
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comparison of different CDPS-containing biosynthetic pathways, the enzyme encoded by amir_4627 is involved in the dimethyl-cyclo-Trp-Trp (cWW) (Me2-cWW) biosynthetic pathway, it possesses an additional intrinsic methyltransferase activity, overview
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metabolism
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comparison of different CDPS-containing biosynthetic pathways, the enzyme encoded by amir_4627 is involved in the dimethyl-cyclo-Trp-Trp (cWW) (Me2-cWW) biosynthetic pathway, it possesses an additional intrinsic methyltransferase activity, overview
-
metabolism
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comparison of different CDPS-containing biosynthetic pathways, the enzyme encoded by amir_4627 is involved in the dimethyl-cyclo-Trp-Trp (cWW) (Me2-cWW) biosynthetic pathway, it possesses an additional intrinsic methyltransferase activity, overview
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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
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
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
physiological function
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the enzyme is a tryptophan-containing cyclodipeptide synthase
physiological function
the enzyme is a tryptophan-containing cyclodipeptide synthase
physiological function
the enzyme is a tryptophan-containing cyclodipeptide synthase
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
physiological function
the enzyme is a tryptophan-containing cyclodipeptide synthase. NcdA catalyzes cyclo(L-Trp-L-Trp) biosynthesis from tryptophanyl-tRNA and does not accept other aromatic aminoacyl-tRNA substrates
physiological function
the enzyme is a tryptophan-containing cyclodipeptide synthase. NozA catalyzes cyclo(L-Trp-L-Trp) biosynthesis from tryptophanyl-tRNA and does not accept other aromatic aminoacyl-tRNA substrates
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
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
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
-
physiological function
Streptomyces lavendulae NRRL B-2774
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
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
-
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
-
physiological function
Streptomyces purpureus NRRL B-5737
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the enzyme is a tryptophan-containing cyclodipeptide synthase
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
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both NozA and NcdA include an active site serine residue that is conserved among characterized CDPSs
additional information
both NozA and NcdA include an active site serine residue that is conserved among characterized CDPSs
additional information
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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
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
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
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
-
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
-
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
-
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
-