L-tryptophan Decarboxylase

A L-tryptophan Decarboxylase is a Psilocybin Biosynthesis Enzyme that decarboxylates L-tryptophan to tryptamine.

• AKA: Decarboxylase PsiD, PSID Gene, L-tryptophan Decarboxylase Enzyme.
• Context:
  • Enzyme Commission Number: 4.1.1.105
  • UniProtKB : P0DPA6
  • Kyoto Encyclopedia of Genes and Genomes: K22433 EC: 4.1.1.105
• Counter-Example(s):
  • Kinase psiK.
  • Cytochrome P450 Monooxygenase psiH,
  • Methyltransferase psiM.
• See: Enzyme, Psilocybin, Psilocybe Cubensis, Decarboxylation.

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References

2019a

• (Uniprot, 2019) ⇒ https://www.uniprot.org/uniprot/P0DPA6 Retrieved:2019-8-3.
  • QUOTE: L-tryptophan decarboxylase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product (PubMed:28763571). The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD (PubMed:28763571). 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well (PubMed:28763571). The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine (PubMed:28763571). The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin (PubMed:28763571). The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin (PubMed:28763571). PsiK kinase can also turn psilocin into psilocybin (PubMed:28763571). This activity may represent a protective mechanism to rephosphorylate the unstable psilocin to the stable psilocybin in case of intracellular ester cleavage (PubMed:28763571).

2019b

• (MetaCyc, 2019) ⇒ https://biocyc.org/gene?orgid=META&id=G-58122 Retrieved:2019-8-3.
  • QUOTE: The psiD gene of Psilocybe cubensis is located in a gene cluster that encodes psilocybin biosynthesis. Sequence analysis suggested that the gene encodes a protein that belongs to the PLP-independent phosphatidylserine decarboxylase family. The protein is not related to PLP-dependent aromatic L-amino acid decarboxylases (EC 4.1.1.28) Fricke17.

    The gene was cloned with an N-terminal His6 tag and expressed in Escherichia coli, and the recombinant protein was purified. Assays with the purified protein have shown that the enzyme catalyzes the decarboxylation of both L-tryptophan and 4-hydroxy-L-tryptophan Fricke17.

2017

• (Fricke et al., 2017) ⇒ Janis Fricke, Felix Blei, and Dirk Hoffmeister (2017). "Enzymatic synthesis of psilocybin". Angewandte Chemie International Edition, 56(40), 12352-12355.
  • QUOTE: . We characterized four psilocybin biosynthesis enzymes, namely i) PsiD, which represents a new class of fungal l-tryptophan decarboxylases, ii) PsiK, which catalyzes the phosphotransfer step, iii) the methyltransferase PsiM, catalyzing iterative N-methyl transfer as the terminal biosynthetic step, and iv) PsiH, a monooxygenase.

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