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运动发酵单胞菌的葡萄糖酸激酶:分离与特性

Gluconate kinase from Zymomonas mobilis: isolation and characteristics.

作者信息

Zachariou M, Scopes R K

出版信息

Biochem Int. 1985 Mar;10(3):367-71.

PMID:2990475
Abstract

The enzyme gluconate kinase EC 2.7.1.12 has been found at high levels in glucose-grown Zymomonas mobilis cells. A simple procedure, based on differential dye-ligand chromatography, has been used to isolate the enzyme, purifying it some 600-fold. The purified enzyme is a monomer of molecular weight 18,000 Da, which is much smaller than other gluconate kinases reported. It has a relatively low affinity for ATP. (Km = 1.5 mM), but high for gluconate (Km = 0.33 mM), and has little activity with any other potential substrates.

摘要

已发现葡萄糖酸激酶(EC 2.7.1.12)在葡萄糖培养的运动发酵单胞菌细胞中含量很高。基于差异染料配体色谱法的一种简单程序已被用于分离该酶,将其纯化了约600倍。纯化后的酶是一种分子量为18,000道尔顿的单体,比报道的其他葡萄糖酸激酶小得多。它对ATP的亲和力相对较低(Km = 1.5 mM),但对葡萄糖酸的亲和力较高(Km = 0.33 mM),并且对任何其他潜在底物的活性都很低。

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