I. Thiebartfassy et Jf. Hervagault, VARIOUS VECTORIAL BEHAVIORS OF A SPATIALLY STRUCTURED SUBSTRATE CYCLE, European journal of biochemistry, 223(3), 1994, pp. 965-969
The dynamic properties of the glucose/glucose-6-phosphate cycle are st
udied under conditions where the phosphatase and kinase interconvertin
g enzymes an spatially distributed. A semi-artificial membrane made of
compacted plant cell walls bearing active phosphatase in its natural
state, separates two compartments, one of these compartments containin
g soluble hexokinase. Depending only upon the two enzyme activity leve
ls and the initial distribution of the substrates, numerous asymmetric
al and vectorial behaviours can be observed, such as facilitated gluco
se 6-phosphate diffusion, active transport of either glucose or glucos
e B-phosphate and sequential (alternative) transport between glucose a
nd glucose 6-phosphate, A diffusion-partition reaction coupling can ac
count for these oriented mass transfers. The possibility of such a cou
pling in this model system is clearly dictated by the global analog of
the Curie principle. These results may provide new insight on (a) the
still obscure role played by the cell-wall phosphatase activities, pa
rticularly their involvement in the transport of exogenous phosphomono
esters, and (b) the actual in vivo operation of substrate and protein
cycles in view of the heterogeneity and anisotropy of the cellular mil
ieu.