2NPX

NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE

2NPX の概要

• エントリーDOI: 10.2210/pdb2npx/pdb
• 分子名称: NADH PEROXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase(h2o2(a))
• 由来する生物種: Enterococcus faecalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51100.20

構造登録者

Stehle, T.,Claiborne, A.,Schulz, G.E. (登録日: 1992-05-29, 公開日: 1994-01-31, 最終更新日: 2024-06-05)

主引用文献

Stehle, T.,Claiborne, A.,Schulz, G.E.
NADH binding site and catalysis of NADH peroxidase.
Eur.J.Biochem., 211:221-226, 1993

PubMed Abstract: The structure of the complex between cofactor NADH and the enzyme NADH peroxidase from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been determined by crystal soaking, X-ray data collection, model building of NADH and refinement at 0.24-nm resolution based on the known enzyme structure [Stehle, T., Ahmed, S. A., Claiborne, A. & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344]. Apart from NADH, the catalytic center of the enzyme contains FAD and a cysteine that shuttles between thiolate and sulfenic acid states. Unfortunately, this cysteine was irreversibly oxidized to a cysteine sulfonic acid in the established enzyme structure. Based on the geometry of the catalytic center, we discuss the stabilization of the oxidation-sensitive sulfenic acid and propose a reaction mechanism.

PubMed: 8425532
DOI: 10.1111/j.1432-1033.1993.tb19889.x

実験手法

X-RAY DIFFRACTION (2.4 Å)