Ligand operated enzyme

The insulin receptor protein represents a ligand-operated enzyme (C), a catalytic receptor. When insulin binds to the extracellular attachment site, a tyrosine kinase activity is "switched on at the intracellular portion. Protein phosphorylation leads to altered cell function via the assembly of other signal proteins. Receptors for growth hormones also belong to the catalytic receptor class. 

Figure 2.5. The synapse. GPCR = guanine nucleotide-binding protein-coupled receptor, LGICR = ligand-gated ion channel receptor, SB = synaptic bouton, T = neurotransmitter, YOC = voltage-operated ion channel protein, YOCC = voltage-operated calcium channel protein, Ast = astrocyte, AA = axoaxonal synapse, ASD = axosomatic or axodendritic synapse. GPCR 1 = receptor protein, 2 = G-protein, 3 = enzyme, 4 = ion channel protein.

As can be concluded from this short description of the factors influencing the overall reaction rate in liquid-solid or gas-solid reactions, the structure of the stationary phase is of significant importance. In order to minimize the transport limitations, different types of supports were developed, which will be discussed in the next section. In addition, the amount of enzyme (operative ligand on the surface of solid phase) as well as its activity determine the reaction rate of an enzyme-catalyzed process. Thus, in the following sections we shall briefly describe different types of chromatographic supports, suited to provide both the high surface area required for high enzyme capacity and the lowest possible internal and external mass transfer resistances. 

It is unknown what role is played by ligand environments in proteins and in synthetic analogues in stabilizing different species as it is also unknown which species represent active oxidants capable of transfering oxygen atoms to substrate in the enzyme systems. Moreover, it is not known how a binuclear metal active site might differ tom a mononuclear active site or if there is one type of reaction mechanism that operates in all or most of the monooxygenase enzymes or if each type of enzyme follows a different mechanism. 

The homogeneous hydrogenation systems discussed in this paper may be treated as analogues of enzyme systems with the rhodium catalyst as the enzyme (E), hydrogen (Si) and cyclohexene (S2) as the substrates, and excess ligand or other donor site as the inhibitor (I). The well-established mathematical operations of enzyme kinetics (12) can then be used to derive rate equations for various possible mechanisms. 

---