Isolation of a cDNA for chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
Isolation of a cDNA for chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
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鸡肝 6-磷酸果糖-2-激酶/果糖-2,6-双磷酸酶 cDNA 的分离。
DOI：
10.1006/bbrc.1993.1061
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发表时间：
1993
影响因子：
3.1
通讯作者：
Pilkis,SJ
中科院分区：
文献类型：
--
作者：
Li,L;Lange,AJ;Pilkis,SJ
鸡肝脏6-磷酸果糖-2-激酶/果糖-2，6的cDNA。从λ ZAP 2噬菌体文库中分离双磷酸酶。鸡肝脏cDNA编码的蛋白质与人、大鼠和牛肝脏同种型分别具有89.1、88.4和88.0%的氨基酸同一性。在大肠杆菌中表达后纯化至均一的大鼠和鸡肝酶的动力学性质。结果表明，Mg ~（2+）对鸡肝6-磷酸果糖-2-激酶（6-phosphofructo-2-kinase，6-phosphofructase，鸡和大鼠肝激酶结构域中β环ATP特征序列的差异可以解释动力学差异，并代表酶从鸟类进化到哺乳动物的主要差异。
A chicken liver cDNA for 6-phosphofructo-2-kinase/fructose-2,6. bisphosphatase was isolated from a Lambda ZAP2 phage library. The chicken liver cDNA codes for a protein that has 89.1, 88.4 and 88.0% amino acid identity with the human, rat and bovine liver isoforms, respectively. The kinetic properties of the rat and chicken liver enzymes, purified to homogeneity after expression inE. coli, were different including negative cooperativity for ATP binding and inhibition by Mg2+for the chicken liver 6-phosphofructo-2-kinase but not for the rat liver kinase. Differences in the β-loop ATP signature sequences in the chicken and rat liver kinase domains may explain the kinetic differences and represent the major divergence in the evolution of the enzyme from birds to mammals.