Chloroplast phosphoribulokinase associates with yeast phosphoriboisomerase in the presence of substrate.
Pea chloroplastic phosphoribulokinase and yeast phosphoriboisomerase partition independently of one another in a two-phase polyethyleneglycol, dextran system, but apparent interaction is seen when ribose-5-phosphate is added to the two-phase system. It appears that the pea leaf kinase recognizes yeast isomerase when it is carrying metabolite.
Skrukrud
C L
CL
Department of Biological Sciences, University of Illinois, Chicago 60680.
Anderson
L E
LE
D019747:Aldose-Ketose Isomerases; D002175:Candida / Q000201:enzymology*; D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology*; D003911:Dextrans; D007887:Fabaceae / Q000201:enzymology*; D010770:Phosphotransferases / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D010946:Plants, Medicinal; D011092:Polyethylene Glycols; D013379:Substrate Specificity
D003911:Dextrans; D011092:Polyethylene Glycols; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022390:phosphoribulokinase; D002238:Carbohydrate Epimerases; D019747:Aldose-Ketose Isomerases; C022548:ribosephosphate isomerase