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Literature summary for 4.2.1.122 extracted from

  • Herger, M.; Van Roye, P.; Romney, D.; Brinkmann-Chen, S.; Buller, A.; Arnold, F.
    Synthesis of beta-branched tryptophan analogues using an engineered subunit of tryptophan synthase (2016), J. Am. Chem. Soc., 138, 8388-8391 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.122

Protein Variants

Protein Variants Comment Organism
I16V/E17G/Q89L/F95L/T292S/V384A site-directed mutagenesis, the mutant PfTrpB2B9 exhibits a 6000fold higher activity with L-Thr compared to wild-type Pyrococcus furiosus
I16V/Q89L site-directed mutagenesis Pyrococcus furiosus
additional information 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 Pyrococcus furiosus
T292S site-directed mutagenesis, the mutant exhibits a 6fold higher activity with L-Thr compared to wild-type Pyrococcus furiosus
T292S/E17G/I68V/F274S/T321A site-directed mutagenesis, the mutant exhibits a 660old higher activity with L-Thr compared to wild-type Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine + indole Pyrococcus furiosus
-
 L-tryptophan + H2O
-
 ?
L-threonine + indole Pyrococcus furiosus
-
 (2S,3S)-beta-methyltryptophan + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + indole
-
 Pyrococcus furiosus L-tryptophan + H2O
-
 ?
L-serine + indole L-serine is the preferred substrate Pyrococcus furiosus L-tryptophan + H2O
-
 ?
L-threonine + 7-azaindole engineered mutant enzyme PfTrpB2B9 Pyrococcus furiosus (2S,3S)-2-amino-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)butanoic acid + H2O
-
 ?
L-threonine + indole
-
 Pyrococcus furiosus (2S,3S)-beta-methyltryptophan + H2O
-
 ?
L-threonine + indole veryl low activity of the wild-type enzyme, higher activity with engineered mutant enzymes Pyrococcus furiosus (2S,3S)-beta-methyltryptophan + H2O
-
 ?
additional information no activity of engineered mutant enzyme with 5-chloro-, 5-bromo, and 6-hydroxyindoles combined with L-threonine Pyrococcus furiosus ?
-
 ?

Synonyms

Synonyms Comment Organism
PfTrpB
-
 Pyrococcus furiosus