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Literature summary for 2.5.1.B31 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
Search for more literature for 2.5.1.B31

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.49
-
 L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus clavatus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, required Aspergillus clavatus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Aspergillus clavatus
-
-
-
Streptomyces coelicolor
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 5-(pent-2-enyl)-L-tryptophan
-
 ?
2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 6-(pent-2-enyl)-L-tryptophan
-
 ?
2-pentenyl diphosphate + L-tryptophan C-6 prenylation Aspergillus clavatus diphosphate + 6-(pent-2-enyl)-L-tryptophan
-
 ?
2-pentenyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 7-(pent-2-enyl)-L-tryptophan
-
 ?
benzyl diphosphate + L-tryptophan C-5 prenylation Aspergillus clavatus diphosphate + 5-benzyl-L-tryptophan
-
 ?
benzyl diphosphate + L-tryptophan C-6 prenylation Streptomyces coelicolor diphosphate + 6-benzyl-L-tryptophan
-
 ?
benzyl diphosphate + L-tryptophan C-6 prenylation Aspergillus clavatus diphosphate + 6-benzyl-L-tryptophan
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
dimethylallyl diphosphate + beta-homo-L-tryptophan 48.8% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
dimethylallyl diphosphate + DL-indole-3-lactic acid 67.3% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
dimethylallyl diphosphate + indole-3-propionic acid 70.7% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
dimethylallyl diphosphate + L-abrine 90.9% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
dimethylallyl diphosphate + L-o-Tyr C-3 prenylation Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-o-tyrosine 3-dimethylallyl-L-tyrosine ?
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
-
 ?
dimethylallyl diphosphate + L-tryptophan
-
 Streptomyces coelicolor diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan best substrate Streptomyces coelicolor diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan best substrate Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan C-5 prenylation Aspergillus clavatus diphosphate + 5-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
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
-
 ?
dimethylallyl diphosphate + trans-indole-3-acrylic acid 38.0% of the activity with L-Trp Aspergillus clavatus ?
-
 ?
methylallyl diphosphate + L-tryptophan C-5 and C-6 prenylation Aspergillus clavatus diphosphate + 5-(but-2-enyl)-L-tryptophan
-
 ?
methylallyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 5-(but-2-enyl)-L-tryptophan
-
 ?
methylallyl diphosphate + L-tryptophan C-5 and C-6 prenylation Aspergillus clavatus diphosphate + 6-(but-2-enyl)-L-tryptophan
-
 ?
methylallyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 6-(but-2-enyl)-L-tryptophan
-
 ?
methylallyl diphosphate + L-tryptophan C-5, C-6 and C-7 prenylation Streptomyces coelicolor diphosphate + 7-(but-2-enyl)-L-tryptophan
-
 ?
additional information substrate specificity, overview Streptomyces coelicolor ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Synonyms

Synonyms Comment Organism
5-DMATS
-
 Streptomyces coelicolor
5-DMATS
-
 Aspergillus clavatus
tryptophan C5-prenyltransferase
-
 Aspergillus clavatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Aspergillus clavatus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.013
-
 L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus clavatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Aspergillus clavatus

General Information

General Information Comment Organism
evolution the enzyme belongs to the DMATS superfamily Aspergillus clavatus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0265
-
 L-o-tyrosine pH 7.5, 37°C, recombinant enzyme Aspergillus clavatus