Kinetics of the coupled reaction catalysed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase: Kinetics of a fusion protein of MDH and CS
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Kinetics of the coupled reaction catalysed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase: Kinetics of a fusion protein of MDH and CS. / Pettersson, Henrik; Olsson, Peter; Bülow, Leif; Pettersson, Gösta.
In: European Journal of Biochemistry, Vol. 267, No. 16, 2000, p. 5041-5046 .Research output: Contribution to journal › Article
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T1 - Kinetics of the coupled reaction catalysed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase: Kinetics of a fusion protein of MDH and CS
AU - Pettersson, Henrik
AU - Olsson, Peter
AU - Bülow, Leif
AU - Pettersson, Gösta
PY - 2000
Y1 - 2000
N2 - The mechanistic implications of the kinetic behaviour of a fusion protein of mitochondrial malate dehydrogenase and citrate synthase have been reanalysed in view of predictions based on experimentally determined kinetic parameter values for the dehydrogenase and synthase activities of the protein. The results show that the time-course of citrate formation from malate in the coupled reaction catalysed by the fusion protein can be most satisfactorily accounted for in terms of a free-diffusion mechanism when consideration is taken to the inhibitory effects of NADH and oxaloacetate on the malate dehydrogenase activity. The effect of aspartate aminotransferase on the coupled reaction is likewise fully consistent with that expected for a free-diffusion mechanism. It is concluded that no tenable kinetic evidence is available to support the proposal that the fusion protein catalyses citrate formation from malate by a mechanism involving channelling of the intermediate oxaloacetate.
AB - The mechanistic implications of the kinetic behaviour of a fusion protein of mitochondrial malate dehydrogenase and citrate synthase have been reanalysed in view of predictions based on experimentally determined kinetic parameter values for the dehydrogenase and synthase activities of the protein. The results show that the time-course of citrate formation from malate in the coupled reaction catalysed by the fusion protein can be most satisfactorily accounted for in terms of a free-diffusion mechanism when consideration is taken to the inhibitory effects of NADH and oxaloacetate on the malate dehydrogenase activity. The effect of aspartate aminotransferase on the coupled reaction is likewise fully consistent with that expected for a free-diffusion mechanism. It is concluded that no tenable kinetic evidence is available to support the proposal that the fusion protein catalyses citrate formation from malate by a mechanism involving channelling of the intermediate oxaloacetate.
KW - fusion protein
KW - channelling
KW - malate dehydrogenase
KW - Citrate (si)-Synthase
KW - Oxaloacetic Acid
KW - Recombinant Fusion Proteins
KW - Saccharomyces cerevisiae
KW - NAD
KW - Models, Chemical
KW - Mitochondria
KW - Kinetics
U2 - 10.1046/j.1432-1327.2000.01558.x
DO - 10.1046/j.1432-1327.2000.01558.x
M3 - Article
C2 - 10931186
VL - 267
SP - 5041
EP - 5046
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 16
ER -