1DID

OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE

1DID の概要

• エントリーDOI: 10.2210/pdb1did/pdb
• 分子名称: D-XYLOSE ISOMERASE, 2,5-DIDEOXY-2,5-IMINO-D-GLUCITOL, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: isomerase(intramolecular oxidoreductase)
• 由来する生物種: Arthrobacter sp.
• 細胞内の位置: Cytoplasm: P12070
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86964.43

構造登録者

Collyer, C.A.,Goldberg, J.D.,Blow, D.M. (登録日: 1992-06-04, 公開日: 1993-07-15, 最終更新日: 2024-02-07)

主引用文献

Collyer, C.A.,Blow, D.M.
Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase.
Proc.Natl.Acad.Sci.USA, 87:1362-1366, 1990

PubMed Abstract: Crystallographic studies of D-xylose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5) incubated to equilibrium with substrate/product mixtures of xylose and xylulose show electron density for a bound intermediate. The accumulation of this bound intermediate shows that the mechanism is a non-Michaelis type. Carrell et al. [Carrell, H. L., Glusker, J. P., Burger, V., Manfre, F., Tritsch, D. & Biellmann, J.-F. (1989) Proc. Natl. Acad. Sci. USA 86, 4440-4444] and the present authors studied crystals of the enzyme-substrate complex under different conditions and made different interpretations of the substrate density, leading to different conclusions about the enzyme mechanism. All authors agree that the bound intermediate of the sugar is in an open-chain form. It is suggested that the higher-temperature study of Carrell et al. may have produced an equilibrium of multiple states, whose density fits poorly to the open-chain substrate, and led to incorrect interpretation. The two groups also bound different closed-ring sugar analogues to the enzyme, but these analogues bind differently. A possible explanation consistent with all the data is that the enzyme operates by a hydride shift mechanism.

PubMed: 2304904
DOI: 10.1073/pnas.87.4.1362

実験手法

X-RAY DIFFRACTION (2.5 Å)