7E6H
glucose-6-phosphate dehydrogenase from Kluyveromyces lactis
7E6H の概要
エントリーDOI | 10.2210/pdb7e6h/pdb |
分子名称 | Glucose-6-phosphate 1-dehydrogenase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHANOL, ... (4 entities in total) |
機能のキーワード | glucose-6-phosphate, dehydrogenase, pentose phosphate pathway, kluyveromyces lactis, oxidoreductase |
由来する生物種 | Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 57075.70 |
構造登録者 | |
主引用文献 | Vu, H.H.,Jin, C.,Chang, J.H. Structural basis for substrate recognition of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis. Biochem.Biophys.Res.Commun., 553:85-91, 2021 Cited by PubMed Abstract: Glucose-6-phosphate dehydrogenase is the first enzyme in the pentose phosphate pathway. The reaction catalyzed by the enzyme is considered to be the main source of reducing power for nicotinamide adenine dinucleotide phosphate (NADPH) and is a precursor of 5-carbon sugar used by cells. To uncover the structural features of the enzyme, we determined the crystal structures of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis (KlG6PD) in both the apo form and a binary complex with its substrate glucose-6-phosphate. KlG6PD contains a Rossman-like domain for cofactor NADPH binding; it also presents a typical antiparallel β sheet at the C-terminal domain with relatively the same pattern as those of other homologous structures. Moreover, our structural and biochemical analyses revealed that Lys153 contributes significantly to substrate G6P recognition. This study may provide insights into the structural variation and catalytic features of the G6PD enzyme. PubMed: 33765558DOI: 10.1016/j.bbrc.2021.02.088 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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