title: Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2).
abstract: 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.
authors.affiliation: Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Haren, The Netherlands.
authors.forename: A M
authors.initials: AM
authors.lastname: Alves
authors.forename: G J
authors.initials: GJ
authors.lastname: Euverink
authors.forename: M J
authors.initials: MJ
authors.lastname: Bibb
authors.forename: L
authors.initials: L
authors.lastname: Dijkhuizen
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000595:Amino Acid Sequence; D001483:Base Sequence; D017124:Conserved Sequence; D004269:DNA, Bacterial / Q000737:chemistry; D006019:Glycolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010732:Phosphofructokinase-1 / Q000302:isolation & purification* / Q000378:metabolism; D010802:Phylogeny; D013302:Streptomyces / Q000378:metabolism*
chemical_list: D004269:DNA, Bacterial; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1