活化的脯氨酰4-羟化酶中存在两个亚铁离子。
Two Fe2+ atoms are present in activated prolyl 4-hydroxylase.
作者信息
De Jong L, Kemp A
出版信息
Biochim Biophys Acta. 1982 Dec 6;709(1):142-5. doi: 10.1016/0167-4838(82)90431-9.
PMID:6295488
Abstract
A linear relationship was found between the activity of prolyl 4-hydroxylase (EC 1.14.11.2) and the amount of Fe2+ bound per mol enzyme. At maximal activity (2.1 mumol X min-1 per mg protein) the enzyme contains 2.1 mol Fe2+ specifically bound per mol enzyme tetramer, indicating two Fe2+-binding sites on prolyl 4-hydroxylase. The half-maximal concentration of added Fe2+ for enzyme activity depends on the nature of sulphydryl compounds present in the reaction medium.
摘要
脯氨酰4-羟化酶（EC 1.14.11.2）的活性与每摩尔酶结合的Fe2+量之间呈线性关系。在最大活性时（每毫克蛋白质2.1 μmol·min-1），该酶每摩尔酶四聚体含有2.1摩尔特异性结合的Fe2+，表明脯氨酰4-羟化酶上有两个Fe2+结合位点。酶活性所需添加Fe2+的半数最大浓度取决于反应介质中存在的巯基化合物的性质。
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