喹蛋白甲胺脱氢酶中色氨酸衍生辅因子的晶体学研究。

Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase.

作者信息

Chen L Y, Mathews F S, Davidson V L, Huizinga E G, Vellieux F M, Duine J A, Hol W G

机构信息

Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.

出版信息

FEBS Lett. 1991 Aug 5;287(1-2):163-6. doi: 10.1016/0014-5793(91)80041-z.

DOI:10.1016/0014-5793(91)80041-z

PMID:1879526

Abstract

A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins.

摘要

麦金太尔等人（《科学》（1991年）252卷，817 - 824页）最近提出的色氨酸 - 色氨酰醌（TTQ）模型，被认为是醌蛋白甲胺脱氢酶的辅基，已与来自嗜硫杆菌和反硝化副球菌的这种脱氢酶的电子密度图进行了比较。比较结果表明，TTQ模型能够很好地适配，有力地支持了TTQ确实是这组醌蛋白的辅因子这一观点。