产朊假丝酵母葡萄糖-6-磷酸脱氢酶NADP⁺结合位点的亲和标记
Affinity labelling of the NADP+-binding site of glucose 6-phosphate dehydrogenase from Candida utilis.
作者信息
Bellini T, Signorini M, Dallocchio F, Rippa M
出版信息
Biochem J. 1979 Nov 1;183(2):297-302. doi: 10.1042/bj1830297.
Abstract
- Periodate-oxidized NADP+ inhibits the catalytic activity of glucose 6-phosphate dehydrogenase from Candida utilis, competing with NADP+. 2. Incubation of the enzyme with the coenzyme analogue causes partial reversible inactivation of the enzyme as a result of affinity labelling of the coenzyme-binding site. 3. Some kinetic values of the reaction were calculated. 4. The inactivation can be made irreversible by treatment with NaBH4, which reduces a Schiff base formed between an aldehyde group on the coenzyme analogue and a lysine residue on the enzyme. 5. Complete inactivation can be correlated with the binding of only one inhibitor to each enzyme subunit. 6. The lysine residue involved in the binding of the inhibitor is present at the coenzyme-binding site.
摘要
- 高碘酸盐氧化的NADP⁺抑制产朊假丝酵母葡萄糖6-磷酸脱氢酶的催化活性，与NADP⁺竞争。2. 酶与辅酶类似物温育会导致酶部分可逆失活，这是辅酶结合位点亲和标记的结果。3. 计算了该反应的一些动力学值。4. 用NaBH₄处理可使失活变为不可逆，NaBH₄会还原辅酶类似物上的醛基与酶上赖氨酸残基之间形成的席夫碱。5. 完全失活可能与每个酶亚基仅结合一个抑制剂有关。6. 参与抑制剂结合的赖氨酸残基存在于辅酶结合位点。
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