Abstract
This chapter focuses on the quaternary structure of enzymes. This structure of enzymes covers oligomeric enzymes and complex enzymes. An oligomeric protein is composed of identical subunits called protomers. On closer inspection, this statement must be qualified by saying that the protomers need not be strictly identical, only quasi-identical. The overwhelming majority of oligomeric enzymes are dimers and tetramers. The chapter discusses the number of subunits in oligomeric enzymes and biological roles of oligomeric structure. The next stage in the structural organization of enzymes after true oligomers is occupied by complex enzymes. This term is used to denote enzymes consisting of catalytic and non-catalytic (as a rule, regulatory) subunits. Complex enzymes may be regarded as allosteric enzymes in which the domain building up the binding site for the regulatory effector(s) is separated from the domain accommodating the catalytic site in the sense that it lies in a distinct polypeptide chain. The chapter discusses regulation of these enzymes through non-catalytic subunits.
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