4XTD

Structure of the covalent intermediate E-XMP* of the IMP dehydrogenase of Ashbya gossypii

4XTD の概要

• エントリーDOI: 10.2210/pdb4xtd/pdb
• 分子名称: Inosine-5'-monophosphate dehydrogenase,Inosine-5'-monophosphate dehydrogenase, INOSINIC ACID (3 entities in total)
• 機能のキーワード: oxidoreductase, xmp
• 由来する生物種: Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast); 詳細
• 細胞内の位置: Cytoplasm : Q756Z6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89753.52

構造登録者

Buey, R.M.,Ledesma-Amaro, R.,Balsera, M.,de Pereda, J.M.,Revuelta, J.L. (登録日: 2015-01-23, 公開日: 2015-07-22, 最終更新日: 2024-11-13)

主引用文献

Buey, R.M.,Ledesma-Amaro, R.,Balsera, M.,de Pereda, J.M.,Revuelta, J.L.
Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii.
Appl.Microbiol.Biotechnol., 99:9577-9589, 2015

PubMed Abstract: Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. Thus, IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis, susceptible of manipulation by means of metabolic engineering approaches. Herein, we report the functional and structural characterization of the IMPDH enzyme from the industrial fungus Ashbya gossypii. Our data show that the overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40 % riboflavin production with respect to the wild type. Also, IMPDH disruption results in a 100-fold increase of inosine excretion to the culture media. Our results contribute to the developing metabolic engineering toolbox aiming at improving the production of metabolites with biotechnological interest in A. gossypii.

PubMed: 26150243
DOI: 10.1007/s00253-015-6710-2

実験手法

X-RAY DIFFRACTION (2.05 Å)