Leferink Nicole G H, Heuts Dominic P H M, Fraaije Marco W, van Berkel Willem J H
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands.
Arch Biochem Biophys. 2008 Jun 15;474(2):292-301. doi: 10.1016/j.abb.2008.01.027. Epub 2008 Feb 6.
The VAO flavoprotein family is a rapidly growing family of oxidoreductases that favor the covalent binding of the FAD cofactor. In this review we report on the catalytic properties of some newly discovered VAO family members and their mode of flavin binding. Covalent binding of the flavin is a self-catalytic post-translational modification primarily taking place in oxidases. Covalent flavinylation increases the redox potential of the cofactor and thus its oxidation power. Recent findings have revealed that some members of the VAO family anchor the flavin via a dual covalent linkage (6-S-cysteinyl-8alpha-N1-histidyl FAD). Some VAO-type aldonolactone oxidoreductases favor the non-covalent binding of the flavin cofactor. These enzymes act as dehydrogenases, using cytochrome c as electron acceptor.
VAO黄素蛋白家族是一个快速增长的氧化还原酶家族，其倾向于FAD辅因子的共价结合。在本综述中，我们报告了一些新发现的VAO家族成员的催化特性及其黄素结合模式。黄素的共价结合是一种主要发生在氧化酶中的自催化翻译后修饰。共价黄素化增加了辅因子的氧化还原电位，从而增强了其氧化能力。最近的研究发现，VAO家族的一些成员通过双共价连接（6-S-半胱氨酰基-8α-N1-组氨酰基FAD）固定黄素。一些VAO型醛糖内酯氧化还原酶倾向于黄素辅因子的非共价结合。这些酶作为脱氢酶，使用细胞色素c作为电子受体。
