Roh J H, Wouters J, Depiereux E, Yukawa H, Inui M, Minami H, Suzuki H, Kumagai H
Research Institute of Innovative Technology for the Earth, Soraku-gun, Kyoto, Japan.
Biochem Biophys Res Commun. 2000 Feb 16;268(2):293-7. doi: 10.1006/bbrc.2000.2113.
The FAD-containing tyramine oxidase enzyme and gene from the Gram (+) bacterium Micrococcus luteus were isolated, and computer prediction was used to propose a preliminary 3D model of the protein. A 2.8-kb Sau3AI fragment containing the structural gene of tyramine oxidase was cloned from a M. luteus genomic DNA library. The 1332 bp gene encodes a protein of 443 amino acids, with a calculated molecular mass of 49.1 kDa. The enzyme was found to be a homodimer with a molecular weight of 49,000. It oxidizes tyramine, adrenaline, 3-hydroxytyramine, dopamine, and noradrenaline, and was reversibly inhibited by FAD-containing monoamine oxidase A and B specific inhibitors. Sequence comparison show that tyramine oxidase is smaller than other FAD-amine oxidases but that it contains well-conserved amino acid residues reported in all other FAD-amine oxidases. A hypothetical three-dimensional structure of tyramine oxidase has also been proposed based on secondary structure predictions, threading, and comparative modeling.
从革兰氏阳性菌藤黄微球菌中分离出含黄素腺嘌呤二核苷酸（FAD）的酪胺氧化酶及其基因，并利用计算机预测构建了该蛋白质的初步三维模型。从藤黄微球菌基因组DNA文库中克隆出一个包含酪胺氧化酶结构基因的2.8 kb Sau3AI片段。该1332 bp的基因编码一个由443个氨基酸组成的蛋白质，计算分子量为49.1 kDa。该酶为同型二聚体，分子量为49,000。它能氧化酪胺、肾上腺素、3-羟基酪胺、多巴胺和去甲肾上腺素，并被含FAD的单胺氧化酶A和B特异性抑制剂可逆抑制。序列比较表明，酪胺氧化酶比其他FAD-胺氧化酶小，但它含有所有其他FAD-胺氧化酶中报道的保守氨基酸残基。还基于二级结构预测、穿线法和比较建模提出了酪胺氧化酶的假设三维结构。
