酪氨酸衍生的醌辅因子。

Tyrosine-derived quinone cofactors.

作者信息

Mure Minae

机构信息

Department of Chemistry, University of California, Berkeley, California 94720, USA.

出版信息

Acc Chem Res. 2004 Feb;37(2):131-9. doi: 10.1021/ar9703342.

DOI:10.1021/ar9703342

PMID:14967060

Abstract

Copper amine oxidases (CAOs) and lysyl oxidase (LOX) both contain Cu(2+) and quinone cofactors that are derived from a tyrosine residue in the active site. In CAOs, the cofactor is 2,4,5-trihydroxyphenylalanine quinone (TPQ), and in LOX it is lysine tyrosyl quinone (LTQ). The mechanism of oxidative deamination by CAOs is well understood, but there is a controversy surrounding the role of Cu(2+) in cofactor reoxidation. The chemistry of LTQ in LOX, by contrast, has not been as extensively studied. This Account discusses the strategies that CAOs have evolved to control the mobility of TPQ to optimize activity. In addition, some recent studies on CAOs whose active-site Cu(2+) has been replaced with Co(2+) or Ni(2+) are summarized. Finally, there is a discussion on the properties of a model compound of LTQ and their relevance to the chemistry of LOX.

摘要

铜胺氧化酶（CAOs）和赖氨酰氧化酶（LOX）都含有Cu(2+)和醌辅因子，这些辅因子源自活性位点的酪氨酸残基。在CAOs中，辅因子是2,4,5-三羟基苯丙氨酸醌（TPQ），而在LOX中则是赖氨酸酪氨酰醌（LTQ）。CAOs氧化脱氨的机制已得到充分理解，但围绕Cu(2+)在辅因子再氧化中的作用存在争议。相比之下，LOX中LTQ的化学性质尚未得到广泛研究。本综述讨论了CAOs为控制TPQ的流动性以优化活性而进化出的策略。此外，还总结了一些活性位点Cu(2+)已被Co(2+)或Ni(2+)取代的CAOs的最新研究。最后，讨论了LTQ模型化合物的性质及其与LOX化学性质的相关性。