糖核苷酸与游离糖协同使大肠杆菌尿苷二磷酸半乳糖4-表异构酶失活。
The concerted inactivation of Escherichia coli uridine diphosphate galactose 4-epimerase by sugar nucleotide together with a free sugar.
作者信息
Blackburn P, Ferdinand W
出版信息
Biochem J. 1976 May 1;155(2):225-9. doi: 10.1042/bj1550225.
Abstract
- The combined effect of the sugar nucleotides UDP-D-fucose or UDP-D-glucuronic acid together with the free sugars D-fucose or L-arabinose is the inactivation of the Escherichia coli enzyme UDP-galactose 4-epimerase (EC 5.1.3.2). The sugar nucleotide or the free sugar alone or the sugar nucleotide plus 5'-Ump do not inactivate the enzyme. 2. The inactivation of the enzyme by its substrate UDP-D-glucose was not affected by the presence of free sugar. 3. In all cases the inactivation observed follows pseudo-first-order kinetics. 4. A comparison of various sugar nucleotides indicates that the hydroxymethyl group at position 6 of the sugar moiety of the natural substrates is important for substrate binding.
摘要
- 糖核苷酸UDP-D-岩藻糖或UDP-D-葡萄糖醛酸与游离糖D-岩藻糖或L-阿拉伯糖共同作用会使大肠杆菌的UDP-半乳糖4-表异构酶（EC 5.1.3.2）失活。单独的糖核苷酸或游离糖，或糖核苷酸加5'-UMP都不会使该酶失活。2. 其底物UDP-D-葡萄糖对该酶的失活作用不受游离糖存在的影响。3. 在所有情况下，观察到的失活遵循假一级动力学。4. 对各种糖核苷酸的比较表明，天然底物糖部分6位的羟甲基对于底物结合很重要。
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