School of Molecular Bioscience, University of Sydney, Sydney, NSW 2006, Australia.
Biochemistry. 2011 Jun 28;50(25):5718-30. doi: 10.1021/bi200555c. Epub 2011 Jun 3.
Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 Å. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.
枝顶孢氨酸氧化酶（ANAO）具有在含铜和三羟苯丙氨酸醌的胺氧化酶家族中不同寻常的能力，能够氧化大肽和蛋白质中赖氨酸残基的胺侧链。我们在这里表明，与来自酵母巴斯德毕赤酵母的相关酶一样，ANAO 可以促进原弹性蛋白的交联，并氧化 α-酪蛋白蛋白和原弹性蛋白中的赖氨酸残基。ANAO 的晶体结构已被确定到 2.4Å 的分辨率，这是该家族中第一个真菌酶的晶体结构。该酶是一个二聚体，具有含铜胺氧化酶的典型折叠。活性位点是该家族中结构特征酶中最开放的，为其赖氨酸氧化酶样活性提供了一个简单的解释。
