Korzeniewski B, Quant P A
Department of Biochemistry, University of Cambridge, England.
Mol Cell Biochem. 1997 Apr;169(1-2):135-42. doi: 10.1023/a:1006882029611.
We propose a simple mechanism which enables decrease of the free pool of channelled metabolite in static spatial channelling, when the concentration of the enzyme consuming the channelled metabolite is greater than the concentration of the enzyme producing this metabolite. Spatial channelling occurs between two enzymes when the common metabolite is released to a small space between these enzymes and does not from a ternary covalent complex with them, as is the case in covalent (dynamic or static) channelling. The mechanism proposed is qualitatively independent of rate constants, metabolite concentrations as well as other kinetic properties and is quantitatively significant for all physiologically relevant conditions. Calculations show that the free metabolite pool must decrease, when the concentration of the enzyme consuming the channelled metabolite is greater than the enzyme producing it. This mechanism is much more effective than increase in the concentration (or rate constant) of the enzyme consuming the metabolite in the absence of spatial channelling.
我们提出了一种简单的机制，当消耗通道化代谢物的酶的浓度大于产生该代谢物的酶的浓度时，该机制能够在静态空间通道化中降低通道化代谢物的自由池。当共同代谢物释放到这两种酶之间的小空间且不像共价（动态或静态）通道化那样与它们形成三元共价复合物时，空间通道化发生在两种酶之间。所提出的机制在定性上与速率常数、代谢物浓度以及其他动力学性质无关，并且在所有生理相关条件下在定量上都具有重要意义。计算表明，当消耗通道化代谢物的酶的浓度大于产生它的酶的浓度时，自由代谢物池必然会减少。在不存在空间通道化的情况下，这种机制比增加消耗代谢物的酶的浓度（或速率常数）要有效得多。
