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猪肾二胺氧化酶底物特异性的重新研究。

A reinvestigation of the substrate specificity of pig kidney diamine oxidase.

作者信息

Bardsley W G, Hill C M, Lobley R W

出版信息

Biochem J. 1970 Mar;117(1):169-76. doi: 10.1042/bj1170169.

Abstract
  1. The substrate specificity of pig kidney diamine oxidase was reinvestigated with a purer enzyme preparation than has previously been used for this purpose. 2. All substrates were extensively purified before use, and methods of preparation or sources are given, together with R(F) values. 3. The substrate specificity determined differed somewhat from that reported by previous workers and, in addition, the behaviour of several compounds not previously used as substrates is described. 4. A model for enzyme-substrate interaction embodying these observations is formulated. It is suggested that a negatively charged substrate-binding group is situated at 6.0-9.0 A from the oxidizing site. The binding and oxidizing sites are separated by a hydrophobic or methylene-binding site.
摘要
  1. 用比以往用于此目的更纯的酶制剂,对猪肾二胺氧化酶的底物特异性进行了重新研究。2. 所有底物在使用前都进行了广泛纯化,并给出了制备方法或来源以及比移值(R(F)值)。3. 所确定的底物特异性与先前研究者报道的有所不同,此外,还描述了几种以前未用作底物的化合物的行为。4. 构建了一个体现这些观察结果的酶 - 底物相互作用模型。有人提出,一个带负电荷的底物结合基团位于距氧化位点6.0 - 9.0埃处。结合位点和氧化位点由一个疏水或亚甲基结合位点隔开。

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本文引用的文献

2
Diamine oxidase.二胺氧化酶
J Biol Chem. 1951 Jan;188(1):125-36.
3
Observations on the substrate specificity of aminne oxidases.关于胺氧化酶底物特异性的观察
Br J Pharmacol Chemother. 1959 Sep;14(3):364-7. doi: 10.1111/j.1476-5381.1959.tb00258.x.
4
The amine oxidases of mammalian plasma.哺乳动物血浆中的胺氧化酶。
J Physiol. 1959 Mar 3;145(2):384-404. doi: 10.1113/jphysiol.1959.sp006149.
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Crystallization and properties of diamine oxidase from pig kidney.猪肾中二胺氧化酶的结晶及性质
Biochem Biophys Res Commun. 1967 Dec 15;29(5):723-7. doi: 10.1016/0006-291x(67)90277-x.

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