Langley David B, Duff Anthony P, Freeman Hans C, Guss J Mitchell
School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1052-7. doi: 10.1107/S1744309106038814. Epub 2006 Oct 25.
Copper-containing amine oxidases are found in all the major kingdoms of life. They catalyse the oxidation of organic amines in the presence of molecular dioxygen to aldehydes and hydrogen peroxide. The catalytic centres contain a Cu atom and a topaquinone cofactor formed autocatalytically from a tyrosine residue in the presence of Cu and molecular oxygen. The structure of the Cu-containing amine oxidase from Arthrobacter globiformis, which was previously refined at 1.8 A resolution in space group C2 with unit-cell parameters a = 157.84, b = 63.24, c = 91.98 A, beta = 112.0 degrees [Wilce et al. (1997), Biochemistry, 36, 16116-16133], has been re-refined with newly recorded data at 1.55 A resolution. The structure has also been solved and refined at 2.2 A resolution in a new crystal form, space group C2, with unit-cell parameters a = 158.04, b = 64.06, c = 69.69 A, beta = 111.7 degrees.
含铜胺氧化酶存在于所有主要的生命王国中。它们在分子氧存在的情况下催化有机胺氧化为醛和过氧化氢。催化中心包含一个铜原子和一个在铜和分子氧存在下由酪氨酸残基自催化形成的对苯醌辅因子。球形节杆菌含铜胺氧化酶的结构，之前在空间群C2中以1.8 Å分辨率精修，晶胞参数为a = 157.84、b = 63.24、c = 91.98 Å、β = 112.0°[威尔西等人（1997年），《生物化学》，36，16116 - 16133]，现已用新记录的1.55 Å分辨率数据重新精修。该结构也已在新的晶体形式（空间群C2，晶胞参数为a = 158.04、b = 64.06、c = 69.69 Å、β = 111.7°）中以2.2 Å分辨率解析和精修。
