ArticleScientific reports2016
Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.
- Pooled it
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- Covalent Immobilization of Different Enzymes on Hydroxyapatite, an Alternative Green Support.ACS omega · 2025Article
- Association of Enterococcus faecalis and tyrosine decarboxylase gene levels with levodopa pharmacokinetics in Parkinson's disease.NPJ Parkinson's disease · 2025Article
- Functional and Physiological Characterization of Tyrosine Decarboxylases fromInternational journal of molecular sciences · 2024Article
- Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase.Cell reports. Physical science · 2024Article
- Computer-aided design and implementation of efficient biosynthetic pathways to produce high added-value products derived from tyrosine inFrontiers in bioengineering and biotechnology · 2024Article
- Application of artificial intelligence approaches to predict the metabolism of xenobiotic molecules by human gut microbiome.Frontiers in microbiology · 2023Review
- Combined chemoenzymatic strategy for sustainable continuous synthesis of the natural product hordenine.Green chemistry : an international journal and green chemistry resource : GC · 2022Article
- A structural metagenomics pipeline for examining the gut microbiome.Current opinion in structural biology · 2022Review
- Aromatic L-amino acid decarboxylases: mechanistic features and microbial applications.Applied microbiology and biotechnology · 2022Review
- Article
- Roles of α‑synuclein in gastrointestinal microbiome dysbiosis‑related Parkinson's disease progression (Review).Molecular medicine reports · 2021Review
- Development of a colorimetric enzymatic assay method for aromatic biogenic monoamine-producing decarboxylases.Food science and biotechnology · 2021Article
- A model of dopamine and serotonin-kynurenine metabolism in cortisolemia: Implications for depression.PLoS computational biology · 2021Article
- Biochemical characterization of specific Alanine Decarboxylase (AlaDC) and its ancestral enzyme Serine Decarboxylase (SDC) in tea plants (Camellia sinensis).BMC biotechnology · 2021Article
- Structural basis for substrate specificity of l-methionine decarboxylase.Protein science : a publication of the Protein Society · 2021Article
- Expression of the Tyrosine Hydroxylase Gene from Rat Leads to Oxidative Stress in Potato Plants.Antioxidants (Basel, Switzerland) · 2020Article
- Crystal structure ofJournal of advanced research · 2020Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyrosine decarboxylase (TDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme and is mainly responsible for the synthesis of tyramine, an important biogenic amine. In this study, the crystal structures of the apo and holo forms of Lactobacillus brevis TDC (LbTDC) were determined. The LbTDC displays only 25% sequence identity with the only reported TDC structure. Site-directed mutagenesis of the conformationally flexible sites and catalytic center was performed to investigate the potential catalytic mechanism. It was found that H241 in the active site plays an important role in PLP binding because it has different conformations in the apo and holo structures of LbTDC. After binding to PLP, H241 rotated to the position adjacent to the PLP pyridine ring. Alanine scanning mutagenesis revealed several crucial regions that determine the substrate specificity and catalytic activity. Among the mutants, the S586A variant displayed increased catalytic efficiency and substrate affinity, which is attributed to decreased steric hindrance and increased hydrophobicity, as verified by the saturation mutagenesis at S586. Our results provide structural information about the residues important for the protein engineering of TDC to improve catalytic efficiency in the green manufacturing of tyramine.
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