EC Number   |
Protein Variants |
Reference |
|---|
  4.2.1.122 | I16V/E17G/Q89L/F95L/T292S/V384A |
site-directed mutagenesis, the mutant PfTrpB2B9 exhibits a 6000fold higher activity with L-Thr compared to wild-type |
748036 |
| 4.2.1.122 | I16V/Q89L |
site-directed mutagenesis |
748036 |
| 4.2.1.122 | L166A |
site-directed mutagenesis the beta-subunit, the mutant shows altered substrate specificity compared to the wild-type enzyme |
-, 747549 |
| 4.2.1.122 | L166V |
site-directed mutagenesis of the beta-subunit, the mutant shows altered substrate specificity compared to the wild-type enzyme, single-step enzymatic synthesis of beta-methyl-Trp derivatives, overview. Although 2-, 4-, 6- or 7-substituted indoles are accepted by StTrpS beta-L66V, along with L-Thr, 5-subsituted indoles prove to be very poor substrates for the enzyme. Variant beta-L166V can better accommodate L-Thr as a substrate |
-, 747549 |
| 4.2.1.122 | more |
an engineered variant of tryptophan synthase from Salmonella enterica (StTrpS) can catalyse the efficient condensation of L-threonine and various indoles to generate bmTrp and derivatives in a single step. Although L-serine is the natural substrate for TrpS, targeted mutagenesis of the StTrpS active site provides a variant (bL166V) that can better accommodate L-Thr as a substrate. The condensation of L-Thr and indole proceeds with retention of configuration at both alpha- and beta-positions to give (2S,3S)-beta-methyl-Trp |
-, 747549 |
| 4.2.1.122 | more |
biocatalytic production of psilocybin and derivatives in tryptophan synthase-enhanced reactions, in vitro reconstituted indole alkaloid synthesis pathway including enzyme PsiD, PsiK and PsiM, and ATP and S-adenosyl-L-methionine, method, overview. Assays run only with TrpB and PsiD result in identical chromatograms |
747575 |
| 4.2.1.122 | more |
Pyrococcus furiosus enzyme engineering by directed evolution of selected TrpB mutant PfTrpB4D11 results in an modified improved enzyme, L-threonine may substitute for L-serine in the beta-substitution reaction of the engineered subunit of tryptophan synthase yielding (2S,3S)-beta-methyltryptophan (beta-MeTrp) in a single step. The trace activity of the wild-type beta-subunit on this substrate is enhanced more than 1000fold by directed evolution. Structural and spectroscopic data indicate that this increase is correlated with stabilization of the electrophilic aminoacrylate intermediate. The engineered biocatalyst also reacts with a variety of indole analogues and thiophenol for diastereoselective C-C, C-N, and C-S bond forming reactions. The new activity circumvents the 3-enzyme pathway that produces beta-MeTrp in nature and offers a simple and expandable route to preparing derivatives of this valuable building block |
748036 |
| 4.2.1.122 | more |
usage of directed evolution to engineer TrpB from Pyrococcus furiosus (PfTrpB) to retain activity in the absence of its TrpA partner. Further engineering of this stand-alone enzyme achieves tha catalysis the of efficient beta-substitution of L-threonine (Thr), yielding (2S,3S)-beta-methyltryptophan (beta-MeTrp) in a single step |
747116 |
| 4.2.1.122 | T292S |
site-directed mutagenesis, the mutant exhibits a 6fold higher activity with L-Thr compared to wild-type |
748036 |
| 4.2.1.122 | T292S/E17G/I68V/F274S/T321A |
site-directed mutagenesis, the mutant exhibits a 660old higher activity with L-Thr compared to wild-type |
748036 |
