EC Number   |
Protein Variants |
Reference |
|---|
   2.5.1.34 | E89A |
site-directed mutagenesis |
738647 |
| 2.5.1.34 | E89A |
site-directed mutagenesis, the mutant shows a 17% reduction in kcat compared to the wild-type enzyme |
722452 |
| 2.5.1.34 | E89Q |
site-directed mutagenesis, the mutant shows a 400fold reduction in kcat compared to the wild-type enzyme |
722452 |
| 2.5.1.34 | I80F |
site-directed mutagenesis |
738647 |
| 2.5.1.34 | I80F |
the mutant enzyme shows similar catalytic ability as FgaPT2 toward cyclo-D-Trp-L-Tyr |
-, 758673 |
| 2.5.1.34 | K174A |
mutation of active site catalytic residue Lys174 to Ala results in a 20fold drop in the value of kcat, the Lys174Ala produces an unusual reverse-prenylated product, 3a-(2-methylbut-3-en-2-yl)-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid |
726466 |
| 2.5.1.34 | K174A |
site-directed mutagenesis, the mutant shows a 31fold reduction in kcat compared to the wild-type enzyme |
722452 |
| 2.5.1.34 | K174A |
site.directed mutagenesis, the mutant FgaPT2 converts tryptophan mainly to a reversely C3-prenylated derivative, while the regularly C4-prenylated tryptophan is detected as a minor product |
737544 |
| 2.5.1.34 | K174E |
site-directed mutagenesis |
738647 |
| 2.5.1.34 | 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 |
738647 |
