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Literature summary for 2.5.1.34 extracted from

  • Fan, A.; Zocher, G.; Stec, E.; Stehle, T.; Li, S.M.
    Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme (2015), J. Biol. Chem., 290, 1364-1373.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.34

Cloned(Commentary)

Cloned (Comment) Organism
gene 4-DMTAS, recombinant overexpression in Escherichia coli strain BL21 (DE3)pLysS Aspergillus fumigatus

Protein Variants

Protein Variants Comment Organism
E89A site-directed mutagenesis Aspergillus fumigatus
I80F site-directed mutagenesis Aspergillus fumigatus
K174E site-directed mutagenesis Aspergillus fumigatus
K174F site-directed mutagenesis, the FgaPT2 mutant shows a much higher catalytic activity toward L-tyrosine than L-tryptophan compared to the wild-type. The single mutation on the key amino acid switches the tryptophan C4-prenyltransferase to a tyrosine C3-prenylating enzyme Aspergillus fumigatus
K174F/R244E site-directed mutagenesis Aspergillus fumigatus
K174Q site-directed mutagenesis Aspergillus fumigatus
K174W site-directed mutagenesis Aspergillus fumigatus
K174Y site-directed mutagenesis Aspergillus fumigatus
additional information inhibitor screening for L-Tyr prenylation activity, overview Aspergillus fumigatus
R244D site-directed mutagenesis Aspergillus fumigatus
R244E site-directed mutagenesis Aspergillus fumigatus
R244N site-directed mutagenesis Aspergillus fumigatus
R244Q site-directed mutagenesis Aspergillus fumigatus
T102C site-directed mutagenesis Aspergillus fumigatus
T102G site-directed mutagenesis Aspergillus fumigatus
T102R site-directed mutagenesis Aspergillus fumigatus
T102S site-directed mutagenesis Aspergillus fumigatus
T102V site-directed mutagenesis Aspergillus fumigatus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Aspergillus fumigatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + L-tryptophan Aspergillus fumigatus
-
 diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus Q50EL0 gene 4-DMATS
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + 4-amino-L-phenylalanine low activity with the wild-type enzyme, higher activity with the enzyme mutant K174F Aspergillus fumigatus diphosphate + 4-amino-3-(3-methylbut-2-enyl)-L-phenylalanine
-
 ?
dimethylallyl diphosphate + L-tryptophan
-
 Aspergillus fumigatus diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tryptophan preferred enzyme of the wild-type enzyme Aspergillus fumigatus diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
-
 ?
dimethylallyl diphosphate + L-tyrosine low activity with the wild-type enzyme, higher activity with the enzyme mutant K174F Aspergillus fumigatus diphosphate + 3-(3-methylbut-2-enyl)-L-tyrosine
-
 ?
additional information the enzyme catalyzes the C-4 prenylation of L-tryptophan, and also the C-3 prenylation of L-tyrosine, cf. EC 2.5.1.122. Single mutation on the key amino acid switches the tryptophan C4 prenyltransferase to a tyrosine C3-prenylating enzyme, active sites and proposed reaction model of FgaPT2 with substrates L-Tyr and 4-amino-L-phenylalanine, overview Aspergillus fumigatus ?
-
 ?

Synonyms

Synonyms Comment Organism
4-DMATS
-
 Aspergillus fumigatus
FgaPT2
-
 Aspergillus fumigatus

Temperature Optimum [°C]

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

pH Optimum

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