title: Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942.
abstract: Phosphoribulokinase (PRK) was purified to electrophoretic homogeneity from Synechococcus PCC7942 with high specific activity. Molecular masses of the native enzyme and its subunit were 178 and 42 kDa, respectively. Cys-17 and Cys-38 were conserved in the cyanobacterial PRK, but 18 amino acid residues between them were missing among the 40 residues found in higher plant PRKs.
authors.affiliation: Department of Applied Biochemistry, University of Osaka Prefecture, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Wadano
authors.forename: Y
authors.initials: Y
authors.lastname: Kamata
authors.forename: T
authors.initials: T
authors.lastname: Iwaki
authors.forename: K
authors.initials: K
authors.lastname: Nishikawa
authors.forename: T
authors.initials: T
authors.lastname: Hirahashi
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D000458:Cyanobacteria / Q000201:enzymology*; D008969:Molecular Sequence Data; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D017853:Phosphotransferases (Alcohol Group Acceptor); C022390:phosphoribulokinase