PURIFICATION AND KINETIC CHARACTERIZATION OF MANNITOL-1-PHOSPHATE DEHYDROGENASE FROM ASPERGILLUS-NIGER
PURIFICATION AND KINETIC CHARACTERIZATION OF MANNITOL-1-PHOSPHATE DEHYDROGENASE FROM ASPERGILLUS-NIGER
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DOI：
10.1016/0003-9861(81)90496-3
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发表时间：
1981-01-01
影响因子：
3.9
通讯作者：
NIEHAUS, WG
中科院分区：
文献类型：
--
作者：
KISER, RC;NIEHAUS, WG
来自黑曲霉的 1-磷酸甘露醇脱氢酶催化 1-磷酸甘露醇依赖 NAD 氧化为 6-磷酸果糖。该酶经过 800 倍纯化，分子量为 40,000，似乎包含 2 个相同分子量的亚基。该酶对底物甘露醇-1-磷酸、果糖-6-磷酸、NAD 和 NADH 具有高度特异性。动力学机制是具有 2 个死端复合物的随机 Bi-Bi。从动力学参数随pH的变化得出结论，该酶含有1个氨基酸残基，pK.α。 9-10，其参与6-磷酸果糖和另一个氨基酸残基与pK.α的结合。约8.2参与催化作用。
Mannitol-1-phosphate dehydrogenase from A. niger catalyzes the NAD-dependent oxidation of mannitol-1-phosphate to fructose-6-phosphate. The enzyme, purified 800-fold to homogeneity has a MW of 40,000 and appears to contain 2 subunits of equal MW. The enzyme is highly specific for the substrates mannitol-1-phosphate, fructose-6-phosphate, NAD and NADH. The kinetic mechanism is random Bi-Bi with 2 dead-end complexes. From the variation of kinetic parameters with pH it is concluded that the enzyme contains 1 amino acid residue with pK.alpha. 9-10 which is involved in binding of fructose-6-phosphate, and another amino acid residue with pK.alpha. about 8.2 which is involved in catalysis.