Patent classifications
C12Y402/0102
HALOGENATED PSILOCYBIN DERIVATIVES AND METHODS OF USING
Disclosed are novel halogenated psilocybin derivative compounds and pharmaceutical and recreational drug formulations containing the same. The compounds may be produced using a biosynthetic system which comprises cells comprising a psilocybin biosynthetic enzyme complement.
AMINATED PSILOCYBIN DERIVATIVES AND METHODS OF USING
Disclosed are novel aminated psilocybin derivative compounds and pharmaceutical and recreational drug formulations containing the same. The aminated psilocybin derivative compounds may be chemically synthesized.
ENGINEERED SYNTHASE FOR PRODUCTION OF TRYPTOPHAN DERIVATIVES AND INTRANSIGENT SUBSTRATES
This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.
Methods and enzyme catalysts for the synthesis of non-canonical amino acids
The present disclosure provides methods for preparing β-substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a β-substituted serine, and iii) a tryptophan synthase β-subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the β-substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new β-substituted tryptophan analogs are also described.
RECOMBINANT HOST CELLS TO PRODUCE ANTHRANILIC ACID
The present invention relates to a recombinant bacterium genetically modified to produce anthranilic acid and being able to grow in a culture medium lacking tryptophan. It also relates to a method for producing anthranilic acid using said recombinant bacterium.
METHODS AND ENZYME CATALYSTS FOR THE SYNTHESIS OF NON-CANONICAL AMINO ACIDS
The present disclosure provides methods for preparing -substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a -substituted serine, and iii) a tryptophan synthase -subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the -substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new -substituted tryptophan analogs are also described.
Method for the synthesis of tryptophan analogs in aqueous solvents at reduced temperatures
The present disclosure provides methods for preparing tryptophans and tryptophan derivatives. The methods include: combining i) an indole substrate or azulene substrate, ii) a serine substrate, and iii) an engineered tryptophan synthase -subunit (TrpB); and maintaining the resulting mixture under conditions sufficient to form the product compound. The engineered TrpB comprises a PLP binding loop mutation, a helix 1 mutation, a strand 7-8 mutation, or a combination thereof. New TrpB variants are also described.
Engineered synthase for production of tryptophan derivatives and intransigent substrates
This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.
ENGINEERED BETA-SUBUNIT OF TRYPTOPHAN SYNTHASE FOR PRODUCTION OF NON-CANONICAL AMINO ACIDS
This disclosure relates to modified tryptophan synthase and more particularly to modified beta-subunits of tryptophan synthase. The disclosure further relates to cells expressing such modified subunits and methods of producing non-canonical amino acids.
Beta-substituted non-canonical amino acids
The present disclosure provides methods for preparing -substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a -substituted serine, and iii) a tryptophan synthase -subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the -substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new -substituted tryptophan analogs are also described.