64363-86-6

Upstream product

• 54648-79-2 O-Methyl-N,N'-diisopropylisourea 
• 73-22-3 L-Tryptophan 
• 74-88-4 methyl iodide 
• 485-80-3 S-adenosyl-L-methionine 
• 526-31-8 L-abrine 

Downstream Products

• 120-72-9 indole 
• 75-50-3 trimethylamine 

Relevant academic research and scientific papers

L-Hypaphorine and D-hypaphorine: Specific antiacetylcholinesterase activity in rat brain tissue

Acetylcholinesterase (AChEis) inhibitors are used to treat neurodegenerative diseases like Alzheimer's disease (AD). L-Hypaphorine (L-HYP) is a natural indole alkaloid that has been shown to have effects on the central nervous system (CNS). The goal of this research was to synthesize L-HYP and D-HYP and test their anticholinesterasic properties in rat brain regions. L-HYP suppressed acetylcholinesterase (AChE) activity only in the cerebellum, whereas D-HYP inhibited AChE activity in all CNS regions studied. No cytotoxic effect on normal human cells (HaCaT) was observed in the case of L-HYP and D-HYP although an increase in cell proliferation. Molecular modeling studies revealed that D-HYP and L-HYP have significant differences in their binding mode positions and interact stereospecifically with AChE's amino acid residues.

Iterative l-Tryptophan Methylation in Psilocybe Evolved by Subdomain Duplication

Psilocybe mushrooms are best known for their l-tryptophan-derived psychotropic alkaloid psilocybin. Dimethylation of norbaeocystin, the precursor of psilocybin, by the enzyme PsiM is a critical step during the biosynthesis of psilocybin. However, the “magic” mushroom Psilocybe serbica also mono- and dimethylates l-tryptophan, which is incompatible with the specificity of PsiM. Here, a second methyltransferase, TrpM, was identified and functionally characterized. Mono- and dimethylation activity on l-tryptophan was reconstituted in vitro, whereas tryptamine was rejected as a substrate. Therefore, we describe a second l-tryptophan-dependent pathway in Psilocybe that is not part of the biosynthesis of psilocybin. TrpM is unrelated to PsiM but originates from a retained ancient duplication event of a portion of the egtDB gene that encodes an ergothioneine biosynthesis enzyme. During mushroom evolution, this duplicated gene was widely lost but re-evolved sporadically and independently in various genera. We propose a new secondary metabolism evolvability mechanism, in which weakly selected genes are retained through preservation in a widely distributed, conserved pathway.

Ergothioneine biosynthetic methyltransferase EgtD reveals the structural basis of aromatic amino acid betaine biosynthesis

Ergothioneine is an N-α-trimethyl-2-thiohistidine derivative that occurs in human, plant, fungal, and bacterial cells. Biosynthesis of this redox-active betaine starts with trimethylation of the α-amino group of histidine. The three consecutive methyl transfers are catalyzed by the S-adenosylmethionine-dependent methyltransferase EgtD. Three crystal structures of this enzyme in the absence and in the presence of N-α-dimethylhistidineand S-adenosylhomocysteine implicate a preorganized array of hydrophilic interactions as the determinants for substrate specificity and apparent processivity. We identified two active site mutations that change the substrate specificity of EgtD 107-fold and transform the histidine-methyltransferase into a proficient tryptophan-methyltransferase. Finally, a genomic search for EgtD homologues in fungal genomes revealed tyrosine and tryptophan trimethylation activity as a frequent trait in ascomycetous and basidomycetous fungi.

Characterization of amino acid-derived betaines by electrospray ionization tandem mass spectrometry

Betaines belong to the naturally occurring osmoprotectants or compatible solutes present in a variety of plants, animals and microorganisms. In recent years, metabolomic techniques have been emerging as a fundamental tool for biologists because the constellation of these molecules and their relative proportions provide with information about the actual biochemical condition of a biological system. Therefore, identification and characterization of biologically important betaines are crucial, especially for metabolomic studies. Most of the natural betaines are derived from amino acids and related homologues. Although, theoretically, all the amino acids can be converted to corresponding betaines by simple methylation of the amine group, only a few of the amino acid-derived betaines were fully characterized in the literature. Here, we report a combined electrospray ionization tandem and high-resolution mass spectrometry study of all the betaines derived from amino acids, including the isomeric betaines. The decomposition pathway of protonated, sodiated and potassiated molecule ions that enable unambiguous characterization of the betaines including the isomeric betaines and overlapping ionic species of different betaines is distinctive. Copyright

Betaines derived from amino and hydrazino acids as phase transfer catalysts

Betaines derived from α-, β- and γ-amino acids (obtained by alkylation of the corresponding amino acids with O-methyl-N.N'- diisopropylisourea) as well as β-hydrazino acids (prepared by dehydrohalogenative hydrolysis of methyl 3-(2-alkyl-2,2-dimethylhydra

Thermodynamic view of hydrophobic association of side chains of aromatic amino acids

The hydrophobic association constants, K, for the side chains of phenylalanine, tyrosin and tryptophan betains have been evaluated employing the difference in the mode of self-association of the optically pure L-betains and their DL-mixtures and using the