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8JG7

Serine decarboxylase

Summary for 8JG7
Entry DOI10.2210/pdb8jg7/pdb
DescriptorSerine decarboxylase, PYRIDOXAL-5'-PHOSPHATE, ZINC ION, ... (4 entities in total)
Functional Keywordsplp, biosynthetic protein
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains4
Total formula weight191363.50
Authors
Wang, H.,Gong, W. (deposition date: 2023-05-19, release date: 2024-05-22, Last modification date: 2024-12-04)
Primary citationWang, H.,Zhu, B.,Qiao, S.,Dong, C.,Wan, X.,Gong, W.,Zhang, Z.
Structure and evolution of alanine/serine decarboxylases and the engineering of theanine production.
Elife, 12:-, 2024
Cited by
PubMed Abstract: Ethylamine (EA), the precursor of theanine biosynthesis, is synthesized from alanine decarboxylation by alanine decarboxylase (AlaDC) in tea plants. AlaDC evolves from serine decarboxylase (SerDC) through neofunctionalization and has lower catalytic activity. However, lacking structure information hinders the understanding of the evolution of substrate specificity and catalytic activity. In this study, we solved the X-ray crystal structures of AlaDC from (CsAlaDC) and SerDC from (AtSerDC). Tyr of AtSerDC or the corresponding Tyr of CsAlaDC is essential for their enzymatic activity. Tyr of AtSerDC and the corresponding Phe of CsAlaDC determine their substrate specificity. Both CsAlaDC and AtSerDC have a distinctive zinc finger and have not been identified in any other Group II PLP-dependent amino acid decarboxylases. Based on the structural comparisons, we conducted a mutation screen of CsAlaDC. The results indicated that the mutation of L110F or P114A in the CsAlaDC dimerization interface significantly improved the catalytic activity by 110% and 59%, respectively. Combining a double mutant of CsAlaDC with theanine synthetase increased theanine production 672% in an system. This study provides the structural basis for the substrate selectivity and catalytic activity of CsAlaDC and AtSerDC and provides a route to more efficient biosynthesis of theanine.
PubMed: 39287621
DOI: 10.7554/eLife.91046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.85 Å)
Structure validation

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