Alves A M, Euverink G J, Bibb M J, Dijkhuizen L
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Haren, The Netherlands.
Appl Environ Microbiol. 1997 Mar;63(3):956-61. doi: 10.1128/aem.63.3.956-961.1997.
The ATP-dependent phosphofructokinase (ATP-PFK) of Streptomyces coelicolor A3(2) was purified to homogeneity (1,600-fold) and characterized (110 kDa, with a single type of subunit of 40 kDa); it is allosterically inhibited by phosphoenolpyruvate. Cloning of the pfk gene of S. coelicolor A3(2) and analysis of the deduced amino acid sequence (343 amino acids; 36,667 Da) revealed high similarities to the PPi-PFK enzyme from Amycolatopsis methanolica (tetramer, nonallosteric; 70%) and to the allosteric ATP-PFK enzymes from other bacteria, e.g., Escherichia coli (tetramer; 37%) and Bacillus stearothermophilus (tetramer, 41%). Further structural and functional analysis of the two actinomycete PFK enzymes should elucidate the features of these proteins that determine substrate specificity (ATP versus PPi) and allosteric (in)sensitivity.
天蓝色链霉菌A3(2)的ATP依赖性磷酸果糖激酶（ATP-PFK）被纯化至均一状态（1600倍）并进行了特性鉴定（110 kDa，具有单一类型的40 kDa亚基）；它受到磷酸烯醇丙酮酸的变构抑制。天蓝色链霉菌A3(2)的pfk基因的克隆以及推导的氨基酸序列分析（343个氨基酸；36,667 Da）显示，其与甲醇拟无枝酸菌的PPi-PFK酶（四聚体，非变构；70%）以及其他细菌的变构ATP-PFK酶高度相似，例如大肠杆菌（四聚体；37%）和嗜热脂肪芽孢杆菌（四聚体，41%）。对这两种放线菌PFK酶的进一步结构和功能分析应能阐明决定底物特异性（ATP与PPi）和变构（不）敏感性的这些蛋白质的特征。
