8JG7

Serine decarboxylase

8JG7 の概要

• エントリーDOI: 10.2210/pdb8jg7/pdb
• 分子名称: Serine decarboxylase, PYRIDOXAL-5'-PHOSPHATE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: plp, biosynthetic protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 191363.50

構造登録者

Wang, H.,Gong, W. (登録日: 2023-05-19, 公開日: 2024-05-22, 最終更新日: 2024-12-04)

主引用文献

Wang, 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

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

実験手法

X-RAY DIFFRACTION (2.85 Å)