Phosphofructokinases from Lactobacteriaceae

Wolfgang A. Simon, Hans Werner Hofer
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引用次数: 5

Abstract

Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance.

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乳杆菌科的磷酸果糖激酶
嗜热链球菌的磷酸果糖激酶(ATP:d-果糖-6-磷酸1-磷酸转移酶,酶代码EC2.7.1.11)已被纯化。它是由分子量为36000的相同亚基组成的四聚体,并表现出米氏动力学。与来自分类相关细菌的磷酸果糖激酶相比,来自嗜热链球菌的酶在高温下更稳定。此外,已经证明乳杆菌和嗜热脂肪芽孢杆菌的磷酸果糖激酶表现出免疫交叉反应。尽管这些酶的动力学性质和热稳定性明显不同,但这一发现表明它们在结构上非常相似。
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Author index Evidence for exchange of inhibitors which bind to the active site of trypsin The kinetics of unphosphorylated, phosphorylated and proteolytically modified fructose bisphosphatase from rat liver Tripeptidyl carboxypeptidase activity of kininase II (angiotensin-converting enzyme) Location of functional -SH groups in NADPH-cytochrome P-450 reductase from rabbit liver microsomes
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