There has been evidence found for allosteric regulation of SCS. There is a high-affinity GDP-binding site that has been found to regulate the enzyme allosterically. This allosteric regulation actually increases the rate of SCS phosphorylation. Another unusual characteristic of the SCS enzyme is one of its catalytic properties which is called substrate synergism. What this means is that the presence of a substrate for one partial reaction stimulates another partial reaction. In E. coli, since there are two catalytic sites, there is alternating catalytic co-operativity. In other words, when a substrate binds one of the catalytic sites, it facilitates the catalytic events at the other catalytic site. This mechanism of catalysis only holds for E. coli, though. In order for substrate synergism to work in mammals, there needs to be a slightly different mechanism since there is only one catalytic site. In this different mechanism, binding of a substrate to the catalytic site enhances another partial reaction to occur at that same site.

In conclusion, the information being obtained about SCS in mammalian systems is still in the relatively early stages of research. A structure for GTP-specific SCS found in pig hearts was just solved in June of 2000. Because of this, researchers are just starting to find out more about how this enzyme functions in mammalian systems and also figuring out how exactly the catalytic mechanism is able to function in the unusual way it does. In other words, there is still much to be learned about the way it functions in the mammalian system and information can still be perfected in a bacterial system, also.