5T95

Prephenate Dehydrogenase M219T, N222D mutant from Soybean

5T95 の概要

• エントリーDOI: 10.2210/pdb5t95/pdb
• 関連するPDBエントリー: 5T8X 5T9E 5T9F
• 分子名称: Prephenate dehydrogenase 1, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, TYROSINE, ... (4 entities in total)
• 機能のキーワード: dehydrogenase, tyrosine biosynthesis, oxidoreductase
• 由来する生物種: Glycine max (Soybean)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63155.42

構造登録者

Holland, C.K.,Jez, J.M. (登録日: 2016-09-09, 公開日: 2017-06-28, 最終更新日: 2023-10-04)

主引用文献

Schenck, C.A.,Holland, C.K.,Schneider, M.R.,Men, Y.,Lee, S.G.,Jez, J.M.,Maeda, H.A.
Molecular basis of the evolution of alternative tyrosine biosynthetic routes in plants.
Nat. Chem. Biol., 13:1029-1035, 2017

PubMed Abstract: L-Tyrosine (Tyr) is essential for protein synthesis and is a precursor of numerous specialized metabolites crucial for plant and human health. Tyr can be synthesized via two alternative routes by different key regulatory TyrA family enzymes, prephenate dehydrogenase (PDH, also known as TyrA) or arogenate dehydrogenase (ADH, also known as TyrA), representing a unique divergence of primary metabolic pathways. The molecular foundation underlying the evolution of these alternative Tyr pathways is currently unknown. Here we characterized recently diverged plant PDH and ADH enzymes, obtained the X-ray crystal structure of soybean PDH, and identified a single amino acid residue that defines TyrA substrate specificity and regulation. Structures of mutated PDHs co-crystallized with Tyr indicate that substitutions of Asn222 confer ADH activity and Tyr sensitivity. Reciprocal mutagenesis of the corresponding residue in divergent plant ADHs further introduced PDH activity and relaxed Tyr sensitivity, highlighting the critical role of this residue in TyrA substrate specificity that underlies the evolution of alternative Tyr biosynthetic pathways in plants.

PubMed: 28671678
DOI: 10.1038/nchembio.2414

実験手法

X-RAY DIFFRACTION (1.689 Å)