Information on EC 2.3.2.B16 - cyclo-(L-Trp-L-Trp) synthase

A0A0R7QX11

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

12 entries

L-tryptophanyl-tRNATrp + L-alanyl-tRNAAla

tRNATrp + tRNAAla + cyclo(L-tryptophanyl-L-alanyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

8 entries

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

10 entries

L-tryptophanyl-tRNATrp + L-valyl-tRNAVal

tRNATrp + tRNAVal + cyclo(L-tryptophanyl-L-valyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Streptomyces purpureus NRRL B-5737

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Streptomyces xanthophaeus NRRL B-5414

Substrates: -
Products: -

2 L-tryptophanyl-tRNATrp

2 tRNATrp + cyclo(L-tryptophanyl-L-tryptophanyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Streptomyces albofaciens

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-leucyl-tRNALeu

tRNATrp + tRNALeu + cyclo(L-tryptophanyl-L-leucyl)

Streptomyces albofaciens DSM 40268

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Streptomyces lavendulae NRRL B-2774

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

L-tryptophanyl-tRNATrp + L-prolyl-tRNAPro

tRNATrp + tRNAPro + cyclo(L-tryptophanyl-L-prolyl)

Substrates: -
Products: -

Go to Disease Search

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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.

22687051

Congenital Abnormalities

Nasca classification of hemivertebra in five dogs.

21851666

Hyperostosis

Using a multimethod life history approach to navigate the osteological paradox: A case study from Prehispanic Nasca, Peru.

33782949

Infections

Human infection with Trypanosoma cruzi in Nasca, Peru: a seroepidemiological survey.

9394524

Scoliosis

Prognostic significance of the Nasca classification for the long-term course of congenital scoliosis.

12228798

Tuberculosis

A 'cold case' of care: Looking at old data from a new perspective in mummy research.

30120031

Tuberculosis, Miliary

A 'cold case' of care: Looking at old data from a new perspective in mummy research.

30120031

Tuberculosis, Spinal

A 'cold case' of care: Looking at old data from a new perspective in mummy research.

30120031

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

UniProt

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Streptomyces albofaciens

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Streptomyces albofaciens DSM 40268

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UniProt

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Streptomyces lavendulae NRRL B-2774

UniProt

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Streptomyces purpureus NRRL B-5737

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Streptomyces xanthophaeus NRRL B-5414

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UniProt

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

17 entries

metabolism

9 entries

physiological function

22 entries

additional information

9 entries

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

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

evolution

phylogenetic analysis of tryptophan-containing cyclodipeptide synthases

evolution

phylogenetic analysis of tryptophan-containing cyclodipeptide synthases

evolution

Streptomyces lavendulae NRRL B-2774

phylogenetic analysis of tryptophan-containing cyclodipeptide synthases

evolution

evolution

evolution

evolution

Streptomyces purpureus NRRL B-5737

phylogenetic analysis of tryptophan-containing cyclodipeptide synthases

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, 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

metabolism

metabolism

metabolism

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. NozA 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. 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

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

physiological function

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

physiological function

the enzyme is a tryptophan-containing cyclodipeptide synthase

physiological function

the enzyme is a tryptophan-containing cyclodipeptide synthase

physiological function

Streptomyces lavendulae NRRL B-2774

the enzyme is a tryptophan-containing cyclodipeptide synthase

physiological function

physiological function

physiological function

Streptomyces xanthophaeus NRRL B-5414

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

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

A0A0R7QWN6

both NozA and NcdA include an active site serine residue that is conserved among characterized CDPSs

additional information

A0A0R7QX11

both NozA and NcdA include an active site serine residue that is conserved among characterized CDPSs

additional information

additional information

additional information

additional information

additional information

additional information

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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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).

A0A0R7QWN6 pBLAST

A0A0R7QWN6_9ACTN

234

26119

TrEMBL

A0A0R7QX11 pBLAST

A0A0R7QX11_9ACTN

242

26333

TrEMBL

Streptomyces lavendulae subsp. lavendulae

A0A2K8PC82 pBLAST

A0A2K8PC82_STRLA

265

29637

TrEMBL

A0A343VTS2 pBLAST

A0A343VTS2_9ACTN

233

26491

TrEMBL

C6WMU7 pBLAST

C6WMU7_ACTMD

Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101)

233

26282

TrEMBL

other Location (Reliability: 2)

F8JRC6 pBLAST

F8JRC6_STREN

Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)

240

25751

TrEMBL

F8JX03 pBLAST

F8JX03_STREN

Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)

278

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

Go to Purification (commentary) Search

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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

expressed in Escherichia coli BL21(DE3) cells

Streptomyces albofaciens

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

2 entries

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

recombinant overexpression in Escherichia coli

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.D.; Knuckley, B.; Alqahtani, N.; Porwal, S.; Ban, J.; Karty, J.A.; Viswanathan, R.; Lane, A.L.

Two distinct cyclodipeptide synthases from a marine actinomycete catalyze biosynthesis of the same diketopiperazine natural product

ACS Synth. Biol.

547-553

2016

Nocardiopsis sp. CMB-M0232 (A0A0R7QWN6), Nocardiopsis sp. CMB-M0232 (A0A0R7QX11)

26641496

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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

Streptantibioticus cattleyicolor (F8JX03), Streptantibioticus cattleyicolor (F8JRC6), Streptomyces lavendulae (A0A2K8PC82), Streptomyces purpureus, Streptomyces xanthophaeus, Streptomyces sp. NRRL S-1868, Streptantibioticus cattleyicolor NRRL 8057 (F8JX03), Streptantibioticus cattleyicolor NRRL 8057 (F8JRC6), Streptantibioticus cattleyicolor DSM 46488 (F8JX03), Streptantibioticus cattleyicolor DSM 46488 (F8JRC6), Streptantibioticus cattleyicolor ATCC 35852 (F8JX03), Streptantibioticus cattleyicolor ATCC 35852 (F8JRC6), Streptantibioticus cattleyicolor JCM 4925 (F8JX03), Streptantibioticus cattleyicolor JCM 4925 (F8JRC6), Streptantibioticus cattleyicolor NBRC 14057 (F8JX03), Streptantibioticus cattleyicolor NBRC 14057 (F8JRC6), Streptomyces lavendulae NRRL B-2774 (A0A2K8PC82), Streptomyces purpureus NRRL B-5737, Streptomyces xanthophaeus NRRL B-5414

29574613

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Borgman, P.; Lopez, R.; Lane, A.

The expanding spectrum of diketopiperazine natural product biosynthetic pathways containing cyclodipeptide synthases

Org. Biomol. Chem.

2305-2314

2019

Streptomyces youssoufiensis (A0A343VTS2), Actinosynnema mirum (C6WMU7), Streptomyces sp., Actinosynnema mirum DSM 43827 (C6WMU7), Actinosynnema mirum ATCC 29888 (C6WMU7), Actinosynnema mirum NBRC 14064 (C6WMU7), Actinosynnema mirum IMRU 3971 (C6WMU7)

30688950

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