牛肝尿苷二磷酸葡萄糖脱氢酶的半位点氧化
Half-sites oxidation of bovine liver uridine diphosphate glucose dehydrogenase.
作者信息
Franzen J S, Marchetti P, Ishman R, Ashcom J
出版信息
Biochem J. 1978 Aug 1;173(2):701-4. doi: 10.1042/bj1730701.
Abstract
6,6-Dithiodinicotinate shows half-of-the-sites reactivity towards the six catalytic-site thiol groups of bovine liver UDP-glucose dehydrogenase. The reagent introduces three intrasubunit disulphide linkages between catalytic-site thiol groups and non-catalytic-site thiol groups and abrogates 60% of the catalytic activity of the hexameric enzyme; excess 2-mercaptoethanol rapidly restores full catalytic activity. These results show the half-of-the-sites behaviour of the enzyme with the reagent and the presence of a non-catalytic-site thiol group capable of forming a disulphide linkage with a catalytic-site thiol group on the same subunit without irreversible denaturation.
摘要
6,6-二硫代烟酸对牛肝UDP-葡萄糖脱氢酶的六个催化位点硫醇基团表现出半数位点反应性。该试剂在催化位点硫醇基团和非催化位点硫醇基团之间引入了三个亚基内二硫键，并消除了六聚体酶60%的催化活性；过量的2-巯基乙醇能迅速恢复其全部催化活性。这些结果表明该酶与试剂的半数位点行为，以及存在一个非催化位点硫醇基团，它能够在同一亚基上与催化位点硫醇基团形成二硫键而不发生不可逆变性。
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本文引用的文献
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