人二胺氧化酶的一种新晶体形式。
A new crystal form of human diamine oxidase.
作者信息
McGrath Aaron P, Hilmer Kimberly M, Collyer Charles A, Dooley David M, Guss J Mitchell
机构信息
School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):137-42. doi: 10.1107/S1744309109052130. Epub 2010 Jan 27.
Abstract
Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1-3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P2(1)2(1)2(1) with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 A resolution in space group C222(1) with one molecule in the asymmetric unit is reported.
摘要
铜胺氧化酶（CAOs）在自然界中广泛存在，催化伯胺氧化脱氨生成相应的醛。人类有三个有活性的CAO基因（AOC1 - 3）。AOC1编码人二胺氧化酶（hDAO），它是组胺代谢的一线酶。hDAO在CAOs中是独特的，因为它对二胺有明显的底物偏好。最近报道了在空间群P2(1)2(1)2(1)中不对称单元有两个分子的hDAO结构。在此，报道了在空间群C222(1)中不对称单元有一个分子的hDAO结构，其分辨率精修至2.1 Å。
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