ArticlePloS one2010
Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 62 citations in OpenAlex.
- Insect-specific aldehyde synthase governs cuticle strength: a selective insecticide target.Science advances · 2026Article
- 3,4-Dihydroxyphenylacetaldehyde synthase evolved an ordered structure to deliver oxygen to pyridoxal 5'-phosphate for cuticle assembly in the mosquito Aedes aegypti.Nature communications · 2025Article
- Advances in the microbial synthesis of the neurotransmitter serotonin.Applied microbiology and biotechnology · 2023Review
- Article
- Construction of cell factory capable of efficiently converting L-tryptophan into 5-hydroxytryptamine.Microbial cell factories · 2022Article
- Crystal structure ofJournal of advanced research · 2020Article
- Structural basis for divergent and convergent evolution of catalytic machineries in plant aromatic amino acid decarboxylase proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural insights into the catalytic mechanism of Bacillus subtilis BacF.Acta crystallographica. Section F, Structural biology communications · 2020Article
- RNA interference-mediated knockdown of 3, 4-dihydroxyphenylacetaldehyde synthase affects larval development and adult survival in the mosquito Aedes aegypti.Parasites & vectors · 2019Article
- Mechanism-based tuning of insect 3,4-dihydroxyphenylacetaldehyde synthase for synthetic bioproduction of benzylisoquinoline alkaloids.Nature communications · 2019Article
- Structure and Ligands Interactions ofBiomolecules · 2019Article
- Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.Frontiers in molecular biosciences · 2019Review
- Insect ArylalkylamineFrontiers in molecular biosciences · 2018Review
- Experimental Evidence and In Silico Identification of Tryptophan Decarboxylase in Citrus Genus.Molecules (Basel, Switzerland) · 2017Article
- Structural Basis of the Substrate Specificity and Enzyme Catalysis of aFrontiers in molecular biosciences · 2017Article
- Critical Analysis of the Melanogenic Pathway in Insects and Higher Animals.International journal of molecular sciences · 2016Review
- Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding.Scientific reports · 2016Article
- Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.Insect biochemistry and molecular biology · 2015Article
- Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.Biochemistry · 2014Article
- Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases.The Journal of biological chemistry · 2013Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
background3,4-Dihydroxyphenylalanine decarboxylase (DDC), also known as aromatic L-amino acid decarboxylase, catalyzes the decarboxylation of a number of aromatic L-amino acids. Physiologically, DDC is responsible for the production of dopamine and serotonin through the decarboxylation of 3,4-dihydroxyphenylalanine and 5-hydroxytryptophan, respectively. In insects, both dopamine and serotonin serve as classical neurotransmitters, neuromodulators, or neurohormones, and dopamine is also involved in insect cuticle formation, eggshell hardening, and immune responses. PRINCIPAL
findingsIn this study, we expressed a typical DDC enzyme from Drosophila melanogaster, critically analyzed its substrate specificity and biochemical properties, determined its crystal structure at 1.75 Angstrom resolution, and evaluated the roles residues T82 and H192 play in substrate binding and enzyme catalysis through site-directed mutagenesis of the enzyme. Our results establish that this DDC functions exclusively on the production of dopamine and serotonin, with no activity to tyrosine or tryptophan and catalyzes the formation of serotonin more efficiently than dopamine.
conclusionsThe crystal structure of Drosophila DDC and the site-directed mutagenesis study of the enzyme demonstrate that T82 is involved in substrate binding and that H192 is used not only for substrate interaction, but for cofactor binding of drDDC as well. Through comparative analysis, the results also provide insight into the structure-function relationship of other insect DDC-like proteins.
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