来自大肠杆菌的N-乙酰葡糖胺6-磷酸脱乙酰酶的纯化及性质
The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli.
作者信息
White R J, Pasternak C A
出版信息
Biochem J. 1967 Oct;105(1):121-5. doi: 10.1042/bj1050121.
Abstract
- N-Acetylglucosamine 6-phosphate deacetylase and 2-amino-2-deoxy-d-glucose 6-phosphate ketol-isomerase (deaminating) (EC 5.3.1.10, glucosamine 6-phosphate deaminase) of Escherichia coliK(12) have been separated by chromatography on DEAE-cellulose. 2. N-Acetylglucosamine 6-phosphate deacetylase has optimum pH8.5 and K(m) 0.8mm. Glucosamine 6-phosphate is a product of the reaction. There appear to be no essential cofactors. Glucosamine 6-phosphate and fructose 6-phosphate inhibit deacetylation. 3. Glucosamine 6-phosphate deaminase has optimum pH7.0 and K(m) 9.0mm. It is stimulated by N-acetylglucosamine 6-phosphate. 4. We propose that the deacetylase be termed 2-acetamido-2-deoxy-d-glucose 6-phosphate amidohydrolase (EC 3.5.1.-), with acetylglucosamine 6-phosphate deacetylase as a trivial name.
摘要
- 大肠杆菌K(12)的N-乙酰葡糖胺6-磷酸脱乙酰酶和2-氨基-2-脱氧-D-葡糖6-磷酸酮醇异构酶（脱氨基）（EC 5.3.1.10，葡糖胺6-磷酸脱氨酶）已通过DEAE-纤维素柱层析分离。2. N-乙酰葡糖胺6-磷酸脱乙酰酶的最适pH为8.5，米氏常数（K(m)）为0.8mmol。反应产物为葡糖胺6-磷酸。似乎不存在必需的辅因子。葡糖胺6-磷酸和果糖6-磷酸抑制脱乙酰作用。3. 葡糖胺6-磷酸脱氨酶的最适pH为7.0，米氏常数为9.0mmol。它受N-乙酰葡糖胺6-磷酸的刺激。4. 我们建议将脱乙酰酶命名为2-乙酰氨基-2-脱氧-D-葡糖6-磷酸酰胺水解酶（EC 3.5.1.-），将乙酰葡糖胺6-磷酸脱乙酰酶作为俗名。
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