Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942.
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.
Wadano
A
A
Department of Applied Biochemistry, University of Osaka Prefecture, Japan.
Kamata
Y
Y
Iwaki
T
T
Nishikawa
K
K
Hirahashi
T
T
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
D017853:Phosphotransferases (Alcohol Group Acceptor); C022390:phosphoribulokinase