ArticleBMC biotechnology2021
Biochemical characterization of specific Alanine Decarboxylase (AlaDC) and its ancestral enzyme Serine Decarboxylase (SDC) in tea plants (Camellia sinensis).
Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 17 citations in OpenAlex.
- Molecular evolution and functional divergence of CsAlaDC from CsSDC reveal key determinants for theanine biosynthesis in tea plants.Horticulture research · 2026Article
- Characterization of the entry steps in diterpenoid alkaloid biosynthesis.Molecular plant · 2026Article
- The dual fate of L-theanine in tea: Metabolic regulation and processing transformations.Journal of advanced research · 2026Review
- Entry Steps in the Biosynthetic Pathway to Diterpenoid Alkaloids inbioRxiv : the preprint server for biology · 2025Article
- L-Theanine Metabolism in Tea Plants: Biological Functions and Stress Tolerance Mechanisms.Plants (Basel, Switzerland) · 2025Review
- Structure and evolution of alanine/serine decarboxylases and the engineering of theanine production.eLife · 2024Article
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8 authors at 3 institutions in 1 country.
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Abstract
backgroundAlanine decarboxylase (AlaDC), specifically present in tea plants, is crucial for theanine biosynthesis. Serine decarboxylase (SDC), found in many plants, is a protein most closely related to AlaDC. To investigate whether the new gene AlaDC originate from gene SDC and to determine the biochemical properties of the two proteins from Camellia sinensis, the sequences of CsAlaDC and CsSDC were analyzed and the two proteins were over-expressed, purified, and characterized.
resultsThe results showed that exon-intron structures of AlaDC and SDC were quite similar and the protein sequences, encoded by the two genes, shared a high similarity of 85.1%, revealing that new gene AlaDC originated from SDC by gene duplication. CsAlaDC and CsSDC catalyzed the decarboxylation of alanine and serine, respectively. CsAlaDC and CsSDC exhibited the optimal activities at 45 °C (pH 8.0) and 40 °C (pH 7.0), respectively. CsAlaDC was stable under 30 °C (pH 7.0) and CsSDC was stable under 40 °C (pH 6.0-8.0). The activities of the two enzymes were greatly enhanced by the presence of pyridoxal-5'-phosphate. The specific activity of CsSDC (30,488 IU/mg) was 8.8-fold higher than that of CsAlaDC (3467 IU/mg).
conclusionsComparing to CsAlaDC, its ancestral enzyme CsSDC exhibited a higher specific activity and a better thermal and pH stability, indicating that CsSDC acquired the optimized function after a longer evolutionary period. The biochemical properties of CsAlaDC might offer reference for theanine industrial production.
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