Rodney Boyer

Concepts in Biochemistry
Third Edition

Chapter 6:
Enzymes II: Cofactors, Regulation, and Catalytic RNA

Copyright 2006 by John Wiley & Sons, Inc.

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Enzyme and coenzymes

Some enzymes biologically active in their native state Some require cofactors for activity Holoenzyme = apoenzyme (protein) + cofactor Cofactors: metal ions; small organic molecule called coenzymes vitamin derivatives

Enzyme regulation
Enzyme activities in metabolic pathways are subject to regulation Allosteric enzymes regulatory enzymes; - Influenced by noncovalent binding of signal molecules (positive effectors or negative effectors) - Oligomeric (several subunits) - Have both catalytic and regulatory sites

Homotropic allosterism
Substrate and effector are the same type of molecule Several catalytic sites; identical subunits The binding of one substrate to a catalytic site influences the binding of other substrates to the catalytic site (positive cooperativity)

Sigmoidal curve characteristic of positive cooperativity

Heterotropic allosterism
Effector molecule is different from the substrate regulatory subunit and catalytic subunit are different

MWC concerted model of positive cooperativity

Sequential model of positive cooperativity by Koshland

Other forms of enzyme regulation

Covalent modification of enzymes chemical alteration of the enzyme - phosphorylation/dephosphorylation of OH grps of serine, threonine or tyrosine - adenylylation - Reduction of disulfide bonds

 Activation by proteolytic cleavage of a proenzyme Zymogens inactive precursor of enzymes

 Regulation by different molecular forms isoenzymes