ArticleApplied microbiology and biotechnology2021
Biochemical characterization and synthetic application of aromatic L-amino acid decarboxylase from Bacillus atrophaeus.
Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 24 citations in OpenAlex.
- Calcium activation mechanism of a noncanonical aromatic L-amino acid decarboxylase from psilocybin mushroom Psilocybe cubensis.Communications biology · 2026Article
- Review
- De Novo Biosynthesis of Antidepressant Psilocybin in Escherichia coli.Microbial biotechnology · 2025Article
- Diversity of Neurotransmitter-Producing Human Skin Commensals.International journal of molecular sciences · 2024Article
- Sustainable production of the drug precursor tyramine by engineered Corynebacterium glutamicum.Applied microbiology and biotechnology · 2024Article
- γ-Polyglutamic Acid Production, Biocontrol, and Stress Tolerance: Multifunction ofInternational journal of environmental research and public health · 2022Article
- Aromatic L-amino acid decarboxylases: mechanistic features and microbial applications.Applied microbiology and biotechnology · 2022Review
- Fermentative Production of Halogenated Tryptophan Derivatives with Corynebacterium glutamicum Overexpressing Tryptophanase or Decarboxylase Genes.Chembiochem : a European journal of chemical biology · 2022Article
- Construction of cell factory capable of efficiently converting L-tryptophan into 5-hydroxytryptamine.Microbial cell factories · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Aromatic L-amino acid decarboxylases (AADCs) are ubiquitously found in higher organisms owing to their physiological role in the synthesis of neurotransmitters and alkaloids. However, bacterial AADC has not attracted much attention because of its rather limited availability and narrow substrate range. Here, we examined the biochemical properties of AADC from Bacillus atrophaeus (AADC-BA) and assessed the synthetic feasibility of the enzyme for the preparation of monoamine neurotransmitters. AADC-BA was expressed in Escherichia coli BL21(DE3) and the purified enzyme showed a specific activity of 2.6 ± 0.4 U/mg for 10 mM L-phenylalanine (L-Phe) at 37 °C. AADC-BA showed optimal pH and temperature ranges at 7-8 and 37-45 °C, respectively. The K
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