8SCC

Crystal Structure of L-galactose 1-dehydrogenase de Myrciaria dubia

8SCC の概要

• エントリーDOI: 10.2210/pdb8scc/pdb
• 分子名称: L-galactose dehydrogenase (2 entities in total)
• 機能のキーワード: l-galactose 1-dehydrogenase, enzyme, plant protein
• 由来する生物種: Myrciaria dubia
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78694.02

構造登録者

Santillan, J.A.V.,Cabrejos, D.A.L.,Pereira, H.M.,Gomez, J.C.C.,Garratt, R.C. (登録日: 2023-04-05, 公開日: 2024-03-13, 最終更新日: 2024-05-15)

主引用文献

Vargas, J.A.,Sculaccio, S.A.,Pinto, A.P.A.,Pereira, H.D.,Mendes, L.F.S.,Flores, J.F.,Cobos, M.,Castro, J.C.,Garratt, R.C.,Leonardo, D.A.
Structural insights into the Smirnoff-Wheeler pathway for vitamin C production in the Amazon fruit camu-camu.
J.Exp.Bot., 75:2754-2771, 2024

PubMed Abstract: L-Ascorbic acid (AsA, vitamin C) is a pivotal dietary nutrient with multifaceted importance in living organisms. In plants, the Smirnoff-Wheeler (SW) pathway is the primary route for AsA biosynthesis and understanding the mechanistic details behind its component enzymes has implications for plant biology, nutritional science and biotechnology. As part of an initiative to determine the structures of all six core enzymes of the pathway, the present study focusses on three of them from the model system Myrciaria dubia (camu-camu): GDP-D-mannose 3',5'-epimerase (GME), L-galactose dehydrogenase (L-GalDH), and L-galactono-1,4-lactone dehydrogenase (L-GalLDH). We provide insights into substrate and cofactor binding and the conformational changes they induce. The MdGME structure reveals a distorted substrate in the active site, pertinent to the catalytic mechanism. MdL-GalDH shows that the way in which NAD+ association affects loop structure over the active site is not conserved when compared with its homologue from spinach. Finally, the structure of MdL-GalLDH is described for the first time. This allows for the rationalization of previously identified residues which play important roles in the active site or in the formation of the covalent bond with the FAD. In conclusion, this study enhances our understanding of AsA biosynthesis in plants and the information provided should prove useful for biotechnological applications.

PubMed: 38224521
DOI: 10.1093/jxb/erae016

実験手法

X-RAY DIFFRACTION (2.09 Å)