Failure of channelling to maintain low concentrations of metabolic intermediates
Open Access
- 1 January 1991
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 195 (1) , 103-108
- https://doi.org/10.1111/j.1432-1033.1991.tb15681.x
Abstract
Computer modelling has been used to investigate the effect of direct transfer of metabolites between consecutive enzymes (channelling) on the free concentrations of the channelled metabolites. When a channelled intermediate cannot participate in any other reactions, any increase in channelling tends to increase its free concentration, albeit very slightly, unless the increase in net flux brought about by the channel is compensated for by a simultaneous decrease in the activity of the route through the free intermediate, in which case channelling has no effect at all on the free steady-state concentration of the channelled intermediate. If the free intermediate is capable of participating in side reactions, channelling can decrease these side reactions, but only slightly unless virtually all of the final product results from flux through the channel and the rate constants for the direct pathway are virtually zero. In general, channelling appears not to provide a useful mechanism for maintaining intermediate concentrations at low levels.Keywords
This publication has 14 references indexed in Scilit:
- Temporal Analysis of the Transition between Steady StatesPublished by Springer Nature ,1990
- Channelling and Channel Efficiency: Theory and Analytical ImplicationsPublished by Springer Nature ,1990
- Coupled Reactions and Channelling: their Role in the Control of MetabolismPublished by Springer Nature ,1990
- Carbohydrate structure of recombinant human uterine tissue plasminogen activator expressed in mouse epithelial cellsEuropean Journal of Biochemistry, 1989
- Mechanism of 1,3‐bisphosphoglycerate transfer from phosphoglycerate kinase to glyceraldehyde‐3‐phosphate dehydrogenaseEuropean Journal of Biochemistry, 1989
- Reexamination of the kinetics of the transfer of NADH between its complexes with glycerol-3-phosphate dehydrogenase and with lactate dehydrogenase.Proceedings of the National Academy of Sciences, 1988
- A functional five‐enzyme complex of chloroplasts involved in the Calvin cycleEuropean Journal of Biochemistry, 1988
- COMPLEXES OF SEQUENTIAL METABOLIC ENZYMESAnnual Review of Biochemistry, 1987
- Complexes Of Sequential Metabolic EnzymesAnnual Review of Biochemistry, 1987
- Conservation of Solvent Capacity and of EnergyPublished by Elsevier ,1977