Channeling of the intermediates and catalytic facilitation to Rubisco in a multienzyme complex of Calvin cycle enzymes.
Calvin cycle multienzyme complex, consisting of phosphoriboisomerase, phosphoribulokinase and ribulose-1,5-bisphosphate carboxylase (Rubisco), shows ribose-5-phosphate + ATP dependent CO2 fixation activity with a small but discernible lag. Transient time analysis showed that the lag at pH 7 was independent of multienzyme concentration and was significantly lower than the expected transient time calculated from Km and Vmax of the individual enzymes, indicative of channeling of the intermediates in the enzyme complex. Channeling of ribulose-1,5-bisphosphate was found to offer a catalytic advantage to Rubisco. Rubisco shows a decrease in activity during catalysis in ribulose-1,5-bisphosphate dependent CO2 fixation reaction, due to the formation of the catalytic inhibitor. Such a decrease of Rubisco activity was not observed in ribose-5-phosphate + ATP dependent CO2 fixation reaction and the catalytic inhibitor was also not detected. These results suggested that the intermediates are channeled in the complex and channeling offers a catalytic facilitation to Rubisco.
Sainis
J K
JK
Molecular Biology & Agriculture Division, Bhabha Atomic Research Centre, Trombay, Bombay.
Jawali
N
N
D019747:Aldose-Ketose Isomerases; D002238:Carbohydrate Epimerases / Q000378:metabolism; D002384:Catalysis; D009097:Multienzyme Complexes / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000378:metabolism; D018515:Plant Leaves; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D018724:Spinacia oleracea
D009097:Multienzyme Complexes; D017853:Phosphotransferases (Alcohol Group Acceptor); C022390:phosphoribulokinase; D012273:Ribulose-Bisphosphate Carboxylase; D002238:Carbohydrate Epimerases; D019747:Aldose-Ketose Isomerases; C022548:ribosephosphate isomerase