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Literature summary extracted from

  • Fan, A.; Xie, X.; Li, S.M.
    Tryptophan prenyltransferases showing higher catalytic activities for Friedel-Crafts alkylation of o- and m-tyrosines than tyrosine prenyltransferases (2015), Org. Biomol. Chem., 13, 7551-7557.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.B31 0.49
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus clavatus
2.5.1.34 0.47
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.34 0.9
-
L-m-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.80 0.17
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.122 0.58
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus niger

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.B31 Ca2+ activates, required Aspergillus clavatus
2.5.1.34 Ca2+ activates Aspergillus fumigatus
2.5.1.80 Ca2+ activates Aspergillus fumigatus
2.5.1.122 Ca2+ activates Aspergillus niger

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 Streptomyces coelicolor
-
diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
?
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 Aspergillus clavatus C-5 prenylation diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus C-4 prenylation diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus C-7 prenylation diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.122 dimethylallyl diphosphate + L-tyrosine Aspergillus niger O-4 prenylation diphosphate + 4-O-dimethylallyl-L-tyrosine
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.B31 Aspergillus clavatus
-
-
-
2.5.1.B31 Streptomyces coelicolor
-
-
-
2.5.1.34 Aspergillus fumigatus Q50EL0
-
-
2.5.1.80 Aspergillus fumigatus Q4WYG3
-
-
2.5.1.122 Aspergillus niger
-
-
-

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 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 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 Streptomyces coelicolor diphosphate + 6-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 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 + 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-o-tyrosine C-5 prenylation, proposed reaction mechanism, overview. Low activity Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine
-
?
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
-
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 best substrate Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.B31 dimethylallyl diphosphate + L-tryptophan C-5 prenylation Aspergillus clavatus 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 substrate specificity, overview Streptomyces coelicolor ?
-
?
2.5.1.B31 additional information HR-ESI-MS and NMR product analysis. The enzyme catalyzes a regiospecific C-prenylation on the indole ring at C5 of L-Trp. No activity with L-m-tyrosine and L-tyrosine Aspergillus clavatus ?
-
?
2.5.1.B31 additional information no or poor activity with 5-methyl-DL-Trp, 5-bromo-DL-Trp, L-m-Tyr. No activity with 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 Aspergillus clavatus ?
-
?
2.5.1.34 dimethylallyl diphosphate + L-m-tyrosine C-4 and C-6 prenylation, proposed reaction mechanism, overview Aspergillus fumigatus diphosphate + 4-(3-methylbut-2-enyl)-L-m-tyrosine + 6-(3-methylbut-2-enyl)-L-m-tyrosine
-
?
2.5.1.34 dimethylallyl diphosphate + L-o-tyrosine C-5 prenylation, proposed reaction mechanism, overview Aspergillus fumigatus diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine
-
?
2.5.1.34 dimethylallyl diphosphate + L-tryptophan C-4 prenylation Aspergillus fumigatus diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.34 dimethylallyl diphosphate + L-tyrosine C-3 prenylation Aspergillus fumigatus diphosphate + 3-(3-methylbut-2-enyl)-L-tyrosine
-
?
2.5.1.34 additional information HR-ESI-MS and NMR product analysis Aspergillus fumigatus ?
-
?
2.5.1.80 dimethylallyl diphosphate + L-o-tyrosine C-5 prenylation, proposed reaction mechanism, overview Aspergillus fumigatus diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine
-
?
2.5.1.80 dimethylallyl diphosphate + L-tryptophan C-7 prenylation Aspergillus fumigatus diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.80 dimethylallyl diphosphate + L-tyrosine O-4 prenylation Aspergillus fumigatus diphosphate + 5-[(2E)-pent-2-en-1-yl]-L-tryptophan
-
?
2.5.1.80 additional information HR-ESI-MS and NMR product analysis. No activity with L-3-tyrosine Aspergillus fumigatus ?
-
?
2.5.1.122 dimethylallyl diphosphate + L-o-tyrosine C-5 prenylation Aspergillus niger diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine
-
?
2.5.1.122 dimethylallyl diphosphate + L-tryptophan C-7 prenylation Aspergillus niger diphosphate + 7-(3-methylbut-2-enyl)-L-tryptophan
-
?
2.5.1.122 dimethylallyl diphosphate + L-tyrosine O-4 prenylation Aspergillus niger diphosphate + 4-O-dimethylallyl-L-tyrosine
-
?
2.5.1.122 additional information HR-ESI-MS and NMR product analysis. No activity with L-m-tyrosine Aspergillus niger ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.B31 5-DMATS
-
Streptomyces coelicolor
2.5.1.B31 5-DMATS
-
Aspergillus clavatus
2.5.1.B31 tryptophan C5-prenyltransferase
-
Aspergillus clavatus
2.5.1.34 FgaPT2
-
Aspergillus fumigatus
2.5.1.34 tryptophan C4-prenyltransferase
-
Aspergillus fumigatus
2.5.1.80 7-DMATS
-
Aspergillus fumigatus
2.5.1.80 tryptophan C7-prenyltransferase
-
Aspergillus fumigatus
2.5.1.122 TyrPT
-
Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.B31 37
-
assay at Aspergillus clavatus
2.5.1.34 37
-
assay at Aspergillus fumigatus
2.5.1.80 37
-
assay at Aspergillus fumigatus
2.5.1.122 37
-
assay at Aspergillus niger

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.B31 0.013
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus clavatus
2.5.1.34 0.0065
-
L-m-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.34 0.29
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.80 0.045
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.122 0.014
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.B31 7.5
-
assay at Aspergillus clavatus
2.5.1.34 7.5
-
assay at Aspergillus fumigatus
2.5.1.80 7.5
-
assay at Aspergillus fumigatus
2.5.1.122 7.5
-
assay at Aspergillus niger

General Information

EC Number General Information Comment Organism
2.5.1.B31 evolution the enzyme belongs to the DMATS superfamily Aspergillus clavatus
2.5.1.34 evolution the enzyme is part of the DMATS superfamily Aspergillus fumigatus
2.5.1.34 metabolism the enzyme is involved in the biosynthesis of fumigaclavine C Aspergillus fumigatus
2.5.1.80 evolution the enzyme is part of the DMATS superfamily Aspergillus fumigatus
2.5.1.80 metabolism the enzyme is involved in the biosynthesis of astechrome Aspergillus fumigatus
2.5.1.122 evolution the enzyme is part of the DMATS superfamily Aspergillus niger

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.B31 0.0265
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus clavatus
2.5.1.34 0.0072
-
L-m-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.34 0.617
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.80 0.265
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus fumigatus
2.5.1.122 0.0241
-
L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus niger