Rapid kinetics of an N-terminal mutant of cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase.
The transient changes in absorption of visible light upon addition of ribulose 1,5-bisphosphate to Co2(+)-activated ribulose-1,5-bisphosphate carboxylase/oxygenase were used to show altered catalytic properties of a mutant form of the enzyme from Anacystis nidulans. The mutant form of the enzyme had a modified N-terminus and a 10-fold greater Km for ribulose 1,5-bisphosphate than the natural cyanobacterial enzyme.
Brändén
R
R
Department of Biochemistry and Biophysics, University of Göteborg, Sweden.
Keys
A J
AJ
Parry
M A
MA
D002384:Catalysis; D003035:Cobalt / Q000494:pharmacology; D000458:Cyanobacteria / Q000201:enzymology* / Q000235:genetics; D007700:Kinetics; D009154:Mutation; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics / Q000378:metabolism*; D012274:Ribulosephosphates / Q000378:metabolism
D012274:Ribulosephosphates; C001933:ribulose-1,5 diphosphate; D003035:Cobalt; D012273:Ribulose-Bisphosphate Carboxylase