乙醇胺 O - 硫酸盐与 4 - 氨基丁酸转氨酶的反应。
The reaction of ethanolamine O-sulphate with 4-aminobutyrate aminotransferase.
作者信息
Fowler L J, John R A
出版信息
Biochem J. 1981 Jul 1;197(1):149-54. doi: 10.1042/bj1970149.
Abstract
The enzyme-induced or 'suicide' step by which the substrate analogue ethanolamine O-sulphate inactivates 4-aminobutyrate aminotransferase occurs at a rate that is one-tenth that observed for the release of the products of beta-elimination, namely ammonia, acetaldehyde and sulphate. An additional reversible reaction not leading to inactivation can be detected spectrally and this decreases the rates of both beta-elimination and inactivation. This reaction is ascribed to a step on the normal transamination path, although complete transamination does not occur significantly. The 14C moiety of radiolabelled ethanolamine O-sulphate is stably bound to the inactive enzyme in the proportion of 1 mol/mol of active site. The 35S-labelled sulphate moiety is not bound after inactivation, showing that beta-elimination must precede inactivation.
摘要
底物类似物乙醇胺 O-硫酸盐使 4-氨基丁酸转氨酶失活的酶促或“自杀”步骤，其发生速率是β-消除产物（即氨、乙醛和硫酸盐）释放速率的十分之一。可以通过光谱检测到一个不会导致失活的额外可逆反应，这降低了β-消除和失活的速率。尽管没有明显发生完全转氨作用，但该反应被归因于正常转氨途径上的一个步骤。放射性标记的乙醇胺 O-硫酸盐的 14C 部分以每摩尔活性位点 1 摩尔的比例稳定地结合到失活的酶上。失活后，35S 标记的硫酸盐部分未结合，表明β-消除必须先于失活发生。
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