2DPG

COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+

2DPG の概要

• エントリーDOI: 10.2210/pdb2dpg/pdb
• 分子名称: GLUCOSE 6-PHOSPHATE DEHYDROGENASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: oxidoreductase, choh(d) - nad(p), nadp/nad, glucose metabolism
• 由来する生物種: Leuconostoc mesenteroides
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55089.01

構造登録者

Adams, M.J.,Naylor, C.E.,Paludin, S.,Gover, S. (登録日: 1998-04-17, 公開日: 1998-07-15, 最終更新日: 2024-04-03)

主引用文献

Cosgrove, M.S.,Naylor, C.,Paludan, S.,Adams, M.J.,Levy, H.R.
On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase.
Biochemistry, 37:2759-2767, 1998

PubMed Abstract: The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate.

PubMed: 9485426
DOI: 10.1021/bi972069y

実験手法

X-RAY DIFFRACTION (2.5 Å)