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Literature summary extracted from

  • Winkelblech, J.; Liebhold, M.; Gunera, J.; Xie, X.; Kolb, P.; Li, S.
    Tryptophan C5-, C6- and C7-prenylating enzymes displaying a preference for C-6 of the indole ring in the presence of unnatural dimethylallyl diphosphate analogues (2015), Adv. Synth. Catal., 357, 975-986.
No PubMed abstract available

Application

EC Number Application Comment Organism
2.5.1.B31 synthesis potential usage of tryptophan prenylating enzymes as biocatalysts for Friedel-Crafts alkylation Aspergillus clavatus
2.5.1.B31 synthesis potential usage of tryptophan prenylating enzymes as biocatalysts for Friedel-Crafts alkylation Streptomyces coelicolor

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.B31 gene SCO7467, recombinant expression of His8-tagged enzyme in Escherichia coli strain BL21(DE3) Streptomyces coelicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.B31 additional information
-
 additional information Michaelis-Menten kinetics Aspergillus clavatus
2.5.1.B31 additional information
-
 additional information Michaelis-Menten kinetics Streptomyces coelicolor
2.5.1.B31 0.028
-
 2-pentenyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.04
-
 benzyl diphosphate pH 7.5, 37°C Aspergillus clavatus
2.5.1.B31 0.05
-
 dimethylallyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.054
-
 methylallyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.076
-
 dimethylallyl diphosphate pH 7.5, 37°C Aspergillus clavatus
2.5.1.B31 0.11
-
 benzyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.12
-
 methylallyl diphosphate pH 7.5, 37°C Aspergillus clavatus
2.5.1.B31 0.13
-
 2-pentenyl diphosphate pH 7.5, 37°C Aspergillus clavatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.B31 Ca2+ required Aspergillus clavatus
2.5.1.B31 Ca2+ required Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan Aspergillus clavatus
-
 diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan Streptomyces coelicolor
-
 diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan Streptomyces coelicolor A3(2)
-
 diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.B31 Aspergillus clavatus
-
-
-
2.5.1.B31 Streptomyces coelicolor Q9ADJ2 gene SCO7467
-
2.5.1.B31 Streptomyces coelicolor A3(2) Q9ADJ2 gene SCO7467
-
2.5.1.80 Aspergillus fumigatus Q4WYG3 gene 7-DMATS
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.B31 recombinant His8-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.B31 2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 5-(pent-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor A3(2) diphosphate + 5-(pent-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 6-(pent-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 2-pentenyl diphosphate + L-tryptophan C-6 prenylation Aspergillus clavatus diphosphate + 6-(pent-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor A3(2) diphosphate + 6-(pent-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 7-(pent-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 benzyl diphosphate + L-tryptophan C-5 prenylation Aspergillus clavatus diphosphate + 5-benzyl-L-tryptophan
-
 ?
2.5.1.B31 benzyl diphosphate + L-tryptophan C-6 prenylation Aspergillus clavatus diphosphate + 6-benzyl-L-tryptophan
-
 ?
2.5.1.B31 benzyl diphosphate + L-tryptophan C-6 prenylation Streptomyces coelicolor diphosphate + 6-benzyl-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + 1-methyl-L-tryptophan 46.9% of the activity with L-Trp Aspergillus clavatus diphosphate + 1-methyl-5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + 4-methyl-L-tryptophan 56.6% of the activity with L-Trp Aspergillus clavatus diphosphate + 4-methyl-5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + 6-fluoro-L-tryptophan 69.5% of the activity with L-Trp Aspergillus clavatus diphosphate + 6-fluoro-5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + 6-methyl-L-tryptophan 53.2% of the activity with L-Trp Aspergillus clavatus diphosphate + 6-methyl-5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + 6-[(2E)-pent-2-en-1-yl]-L-tryptophan
-
 Streptomyces coelicolor diphosphate + 7-[(2E)-pent-2-en-1-yl]-L-tryptophan + 5-[(2E)-pent-2-en-1-yl]-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + 7-methyl-DL-tryptophan 57.8% of the activity with L-Trp Aspergillus clavatus diphosphate + 7-methyl-5-(3-methylbut-2-enyl)-DL-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + beta-homo-L-tryptophan 48.8% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
2.5.1.B31 dimethylallyl diphosphate + DL-indole-3-lactic acid 67.3% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
2.5.1.B31 dimethylallyl diphosphate + indole-3-propionic acid 70.7% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-abrine 90.9% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-o-Tyr C-3 prenylation Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine 3-dimethylallyl-L-tyrosine ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan
-
 Streptomyces coelicolor diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan best substrate Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan best substrate Streptomyces coelicolor diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan
-
 Streptomyces coelicolor A3(2) diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan best substrate Streptomyces coelicolor A3(2) diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + N-acetyl-DL-tryptophan 54.4% of the activity with L-Trp Aspergillus clavatus diphosphate + N-acetyl-5-(3-methylbut-2-enyl)-DL-tryptophan
-
 ?
2.5.1.B31 dimethylallyl diphosphate + trans-indole-3-acrylic acid 38.0% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
2.5.1.B31 methylallyl diphosphate + L-tryptophan C-5 and C-6 prenylation Aspergillus clavatus diphosphate + 5-(but-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 methylallyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 5-(but-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 methylallyl diphosphate + L-tryptophan C-5 and C-6 prenylation Aspergillus clavatus diphosphate + 6-(but-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 methylallyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 6-(but-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 methylallyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 7-(but-2-enyl)-L-tryptophan
-
 ?
2.5.1.B31 additional information no or poor activity with 5-methyl-DL-Trp, 5-bromo-DL-Trp, L-m-Tyr, and 6-[(2E)-pent-2-en-1-yl]-L-tryptophan. The enzyme catalyzes regiospecific prenylations of indolocarbazoles at the para-position of the indole N-atom. Molecular dynamics simulation experiments with a homologous model of 5-DMATS explain well its reactions with methylallyl and 2-pentenyl diphosphate. Comparison of bacterial and fungal alkylation/benzylation reactions by investigations on 5-DMATS from Aspergillus clavatus and 5-DMATSSc from Streptomyces coelicolor. Homology modelling of 5-DMATS, overview Aspergillus clavatus ?
-
 ?
2.5.1.B31 additional information substrate specificity, overview. Molecular dynamics simulation experiments with a homologous model of 5-DMATS explain well its reactions with methylallyl and 2-pentenyl diphosphate. Comparison of bacterial and fungal alkylation/benzylation reactions by investigations on 5-DMATS from Aspergillus clavatus and 5-DMATSSc from Streptomyces coelicolor. Homology modelling of 5-DMATS, overview Streptomyces coelicolor ?
-
 ?
2.5.1.B31 additional information substrate specificity, overview. Molecular dynamics simulation experiments with a homologous model of 5-DMATS explain well its reactions with methylallyl and 2-pentenyl diphosphate. Comparison of bacterial and fungal alkylation/benzylation reactions by investigations on 5-DMATS from Aspergillus clavatus and 5-DMATSSc from Streptomyces coelicolor. Homology modelling of 5-DMATS, overview Streptomyces coelicolor A3(2) ?
-
 ?
2.5.1.80 additional information the tryptophan C7-prenyltransferase 7-DMATS from Aspergillus fumigatus accepts very poorly methylallyl diphosphate and 2-pentenyl diphosphate as substrates, it shows low activity in the presence of unnatural dimethylallyl diphosphate analogues Aspergillus fumigatus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.B31 5-DMATS
-
 Aspergillus clavatus
2.5.1.B31 5-DMATSSc
-
 Streptomyces coelicolor
2.5.1.B31 SCO7467
-
 Streptomyces coelicolor
2.5.1.B31 tryptophan C5-prenyltransferase
-
 Aspergillus clavatus
2.5.1.B31 tryptophan C5-prenyltransferase
-
 Streptomyces coelicolor
2.5.1.80 7-DMATS
-
 Aspergillus fumigatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.B31 37
-
 assay at Aspergillus clavatus
2.5.1.B31 37
-
 assay at Streptomyces coelicolor

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.B31 0.00028
-
 benzyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.00048
-
 methylallyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.0014
-
 2-pentenyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 0.0015
-
 methylallyl diphosphate pH 7.5, 37°C Aspergillus clavatus
2.5.1.B31 0.005
-
 benzyl diphosphate pH 7.5, 37°C Aspergillus clavatus
2.5.1.B31 0.023
-
 2-pentenyl diphosphate pH 7.5, 37°C Aspergillus clavatus
2.5.1.B31 0.4
-
 dimethylallyl diphosphate pH 7.5, 37°C Streptomyces coelicolor
2.5.1.B31 1.3
-
 dimethylallyl diphosphate pH 7.5, 37°C Aspergillus clavatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.B31 7.5
-
 assay at Aspergillus clavatus
2.5.1.B31 7.5
-
 assay at Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
2.5.1.B31 additional information molecular dynamics simulation experiments with a homologous model of 5-DMATS, overview Aspergillus clavatus
2.5.1.B31 additional information molecular dynamics simulation experiments with a homologous model of 5-DMATS, overview Streptomyces coelicolor