Ontology highlight
ABSTRACT:
SUBMITTER: Alves AM
PROVIDER: S-EPMC168387 | biostudies-other | 1997 Mar
REPOSITORIES: biostudies-other
Applied and environmental microbiology 19970301 3
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 alloste ...[more]