Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli
Purification and characterization of glpX-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli
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DOI：
10.1128/jb.182.19.5624-5627.2000
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发表时间：
2000-10-01
影响因子：
3.2
通讯作者：
Larson, TJ
中科院分区：
文献类型：
--
作者：
Donahue, JL;Bownas, JL;Larson, TJ
在大肠杆菌中，glp的基因产物调节介导甘油和sn-甘油3-磷酸的利用。glpFKX操纵子编码甘油扩散促进剂、甘油激酶，如图所示，它是一种果糖1,6-双磷酸酶，与先前描述的fbp编码酶不同。纯化后的酶是二聚体，依赖于Mn2+的活性，对果糖1,6-二磷酸的表观K-m为35 μ M。ADP和磷酸抑制该酶，磷酸烯醇丙酮酸激活该酶。
In Escherichia coli, gene products of the glp regulon mediate utilization of glycerol and sn-glycerol 3-phosphate. The glpFKX operon encodes glycerol diffusion facilitator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the previously described fbp-encoded enzyme. The purified enzyme was dimeric, dependent on Mn2+ for activity, and exhibited an apparent K-m of 35 mu M for fructose 1,6-bisphosphate. The enzyme was inhibited by ADP and phosphate and activated by phosphoenolpyruvate.