Rodney Boyer

Concepts in Biochemistry
Third Edition

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

Copyright © 2006 by John Wiley & Sons, Inc.

Choline – essential
nutrient
Rapid brain
development, enhance
memory and slows
progression of
Alzheimer’s disease;
improves liver and
cardiovascular
function
Rich sources: fish,
eggs, soybeans, liver,
cauliflower, peanuts
 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
sites influences the binding of the other
substrate 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
Zymogens – inactive precursor of enzymes
• Regulation by different molecular forms -
isoenzymes