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Information on EC 2.3.2.B16 - cyclo-(L-Trp-L-Trp) synthase
for references in articles please use BRENDA:EC2.3.2.B16preliminary BRENDA-supplied EC number
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EC Tree
2.3.2.B16 cyclo-(L-Trp-L-Trp) synthaseSpecify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
nasca, dmtb1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amir_4627
CDPS
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tryptophanyl-tRNATrp + L-alanyl-tRNAAla
tRNATrp + tRNAAla + cyclo(L-tryptophanyl-L-alanyl)
-
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
L-tryptophanyl-tRNATrp + L-valyl-tRNAVal
tRNATrp + tRNAVal + cyclo(L-tryptophanyl-L-valyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
Streptomyces purpureus NRRL B-5737
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
Streptomyces lavendulae NRRL B-2774
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
-
?
additional information
?
-
LC-MS product analysis. No activity with tyrosyl-tRNA, phenylalanyl-tRNA, or combinations of these aa-tRNAs with and without tryptophanyl-tRNA. The enzyme is specific for tryptophanyl-tRNA
-
-
-
additional information
?
-
LC-MS product analysis. No activity with tyrosyl-tRNA, phenylalanyl-tRNA, or combinations of these aa-tRNAs with and without tryptophanyl-tRNA. The enzyme is specific for tryptophanyl-tRNA
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tryptophanyl-tRNATrp + L-alanyl-tRNAAla
tRNATrp + tRNAAla + cyclo(L-tryptophanyl-L-alanyl)
-
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
L-tryptophanyl-tRNATrp + L-valyl-tRNAVal
tRNATrp + tRNAVal + cyclo(L-tryptophanyl-L-valyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
Streptomyces purpureus NRRL B-5737
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
2 L-tryptophanyl-tRNATrp
2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)
-
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu
tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
Streptomyces lavendulae NRRL B-2774
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
-
?
L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro
tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)
-
-
-
-
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cataract
NASCA Report 2: Longitudinal Study of Relationship of Exposure to Space Radiation and Risk of Lens Opacity.
Hyperostosis
Using a multimethod life history approach to navigate the osteological paradox: A case study from Prehispanic Nasca, Peru.
Infections
Human infection with Trypanosoma cruzi in Nasca, Peru: a seroepidemiological survey.
Scoliosis
Prognostic significance of the Nasca classification for the long-term course of congenital scoliosis.
Tuberculosis
A 'cold case' of care: Looking at old data from a new perspective in mummy research.
Tuberculosis, Miliary
A 'cold case' of care: Looking at old data from a new perspective in mummy research.
Tuberculosis, Spinal
A 'cold case' of care: Looking at old data from a new perspective in mummy research.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
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
-
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
evolution
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
evolution
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)
-
evolution
-
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)
-
evolution
Streptomyces lavendulae NRRL B-2774
-
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
evolution
-
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)
-
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
Streptomyces purpureus NRRL B-5737
-
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
evolution
-
phylogenetic analysis of tryptophan-containing cyclodipeptide synthases
-
metabolism
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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
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
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
physiological function
-
the enzyme is a tryptophan-containing cyclodipeptide synthase
-
additional information
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2K8PC82_STRLA
265
0
29637
TrEMBL
-
C6WMU7_ACTMD
Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101)
233
0
26282
TrEMBL
-
F8JRC6_STREN
Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)
240
0
25751
TrEMBL
-
F8JX03_STREN
Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)
278
0
29582
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S23A
site-directed mutagenesis, catalytically inactive mutant
S36A
site-directed mutagenesis, catalytically inactive mutant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography, followed by ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dmtB1, recombinant expression of the gene cluster dmtB1-dmtC1 from Streptomyces youssoufiensis in Streptomyces coelicolor results in production of cyclic Trp-Pro, cyclic Trp-Val, and cycic Trp-Leu derivatives with a farnesyl group at indole C-3, dubbed pre-drimentines (e.g. pre-drimentine G = (3S,5aS,10bS,11aS)-3-(propan-2-yl)-10b-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-6,10b,11,11a-tetrahydro-2H-pyrazino[1',2':1,5]pyrrolo[2,3-b]indole-1,4(3H,5aH)-dione)
gene ncdA, genetic organization, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15
gene nozA, genetic organization, sequence comparisons and phylogenetic tree, functional recombinant expression of the noz gene cluster in Streptomyces coelicolor, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15
gene SCATT_09020, phylogenetic analysis, recombinant overexpression in Escherichia coli
gene SCATT_42550, phylogenetic analysis, recombinant overexpression in Escherichia coli
gene SLAV_12475, phylogenetic analysis, recombinant overexpression in Escherichia coli
phylogenetic analysis, recombinant overexpression in Escherichia coli
recombinant expression in Streptomyces coelicolor, recombinant expression of the CDPS in Escherichia coli results in accumulation of cyclo(L-tryptophanyl-L-tryptophanyl) as the sole detectable 2,5-diketopiperazine (DKP) product
-
phylogenetic analysis, recombinant overexpression in Escherichia coli
-
phylogenetic analysis, recombinant overexpression in Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
James, E.; Knuckley, B.; Alqahtani, N.; Porwal, S.; Ban, J.; Karty, J.; Viswanathan, R.; Lane, A.
Two distinct cyclodipeptide synthases from a marine actinomycete catalyze biosynthesis of the same diketopiperazine natural product
ACS Synth. Biol.
5
547-553
2016
Nocardiopsis sp. CMB-M0232 (A0A0R7QWN6), Nocardiopsis sp. CMB-M0232 (A0A0R7QX11)
brenda
Liu, J.; Yu, H.; Li, S.M.
Expanding tryptophan-containing cyclodipeptide synthase spectrum by identification of nine members from Streptomyces strains
Appl. Microbiol. Biotechnol.
102
4435-4444
2018
Streptomyces purpureus, Streptomyces xanthophaeus, Streptomyces sp. NRRL S-1868, Streptomyces lavendulae (A0A2K8PC82), Streptomyces cattleya (F8JRC6), Streptomyces cattleya (F8JX03), Streptomyces cattleya ATCC 35852 (F8JRC6), Streptomyces cattleya ATCC 35852 (F8JX03), Streptomyces cattleya NRRL 8057 (F8JRC6), Streptomyces cattleya NRRL 8057 (F8JX03), Streptomyces lavendulae NRRL B-2774 (A0A2K8PC82), Streptomyces cattleya DSM 46488 (F8JRC6), Streptomyces cattleya DSM 46488 (F8JX03), Streptomyces cattleya JCM 4925 (F8JRC6), Streptomyces cattleya JCM 4925 (F8JX03), Streptomyces xanthophaeus NRRL B-5414, Streptomyces purpureus NRRL B-5737, Streptomyces cattleya NBRC 14057 (F8JRC6), Streptomyces cattleya NBRC 14057 (F8JX03)
brenda
Borgman, P.; Lopez, R.; Lane, A.
The expanding spectrum of diketopiperazine natural product biosynthetic pathways containing cyclodipeptide synthases
Org. Biomol. Chem.
17
2305-2314
2019
Streptomyces sp., Streptomyces youssoufiensis (A0A343VTS2), Actinosynnema mirum (C6WMU7), Actinosynnema mirum NBRC 14064 (C6WMU7), Actinosynnema mirum ATCC 29888 (C6WMU7), Actinosynnema mirum IMRU 3971 (C6WMU7), Actinosynnema mirum DSM 43827 (C6WMU7)
brenda
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Release 2023.1 (January 2023)
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