A novel β-diketone-cleaving enzyme from Acinetobacter johnsonii:: acetylacetone 2,3-oxygenase
A novel β-diketone-cleaving enzyme from Acinetobacter johnsonii:: acetylacetone 2,3-oxygenase
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DOI：
10.1016/s0006-291x(02)02182-4
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发表时间：
2002-09-20
影响因子：
3.1
通讯作者：
Ribbons, DW
中科院分区：
文献类型：
--
作者：
Straganz, G;Brecker, L;Ribbons, DW
强森不动杆菌一种新型的含铁锌加氧酶催化乙酰丙酮2，3-裂解为乙酸酯和乙二醛。反应物和产物的化学计量符合经典的双加氧酶。该纯蛋白是KD的同源四聚体，含有不同量的Fe~(2+)和Zn~(2+)。该酶的活性与Fe2+含量的关系比与蛋白质含量的关系更为密切。本文介绍了乙酰丙酮2，3-加氧酶的纯化方法、部分物理性质以及对类似底物的选择。(C)2002年埃尔塞维尔科学公司(美国)。版权所有。
A novel Fe + Zn containing oxygenase from Acinetobacter johnsonii catalyses 2,3-cleavage of acetylacetone to acetate and methylglyoxal has been purified. The stoichiometry of reactants and products conforms to a classical dioxygenase. The pure protein is a homotetramer of 64 kD with variable amounts of Fe2+ and Zn2+. Activity of the enzyme is more closely related to the Fe2+ content than to the amount of protein. A purification of acetylacetone 2,3-oxygenase, some of its physical properties, and the preference for some analogous substrates are described. (C) 2002 Elsevier Science (USA). All rights reserved.