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4.1.1.105 |
Description |
L-tryptophan decarboxylase |
Alternative names |
psiD (gene name); TDC (gene name) |
Catalyzed reaction |
L-tryptophan = tryptamine + CO(2). |
Cofactor |
Pyridoxal-phosphate or pyruvate. |
Comments |
-!- The enzyme has been characterized from bacteria, plants, and fungi. Unlike EC 4.1.1.28, aromatic-L-amino-acid decarboxylase, this enzyme is specific for L-typtophan. |
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The L-Trp decarboxylase from the fungus Psilocybe (involved in the biosynthesis of the psychotropic psilocybin) is PLP-independent and presumably requires a pyruvoyl group. |
PDB |
4OBV; |
Organisms |
-Eubacteria -Plants -Fungi |
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Family |
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Links |
Enzyme (activities) 4.1.1.105
BRENDA (activities) 4.1.1.105
KEGG (pathways) 4.1.1.105
PLPMDB (PLP mutants) 4.1.1.105
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References |
Fricke J, Blei F, Hoffmeister D (2017) Enzymatic Synthesis of Psilocybin Angew Chem Int Ed Engl 56 12352-12355. Williams BB, Van Benschoten AH, Cimermancic P, Donia MS, Zimmermann M, Taketani M, Ishihara A, Kashyap PC, Fraser JS, Fischbach MA (2014) Discovery and characterization of gut microbiota decarboxylases that can produce the neurotransmitter tryptamine Cell Host Microbe 16 495-503. Yuwen L, Zhang FL, Chen QH, Lin SJ, Zhao YL, Li ZY. (2013) The role of aromatic L-amino acid decarboxylase in bacillamide C biosynthesis by Bacillus atrophaeus C89. Sci Rep. 3 1753. Articles on 4.1.1.105 |
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last changed |
2019/06/21 13:13 |
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