Module 1B SGD Session 1: Cell Bioenergetics

BIOCHHEMISTRY - Dr. Moro-Espidilla (Harper’s)

1. Discuss cell bioenergetics

1.1 Identify descriptions of the different protein-binding sites (receptors)
1.1.1 Identify descriptions of the following: enzymes, co-enzymes, co-factors, isoenzymes,
proenzymes

 Enzymes: biocatalyst; increases the rate of reactions without being used in the process; hasten
the rate by lowering the activation energy of the transitional state (the state with either
reactants and products are formed.
 Some enzymes require molecules other than proteins for enzymatic activity. Enzyme with their
non-protein portion is called apoenzyme and inactive. Active enzymes with their non-protein
component are called holoenzyme.
 Coenzymes: small organic molecule
 Co-factors: metal such as Zn+ or Fe+
 Isoenzymes: different structures AA sequence but catalyze the same chemical reaction

1.1.2 State/identify major groups o enzymes and their examples

 Oxidoreductases- Transfer of electrons (hydride ions or H atoms)

 Transferases - Group transfer reactions
 Hydrolases- Hydrolysis reactions (transfer of functional groups to water)
 Lyases -Addition of groups to double bonds, or formation of double bonds by removal of groups
 Isomerases- Transfer of groups within molecules to yield isomeric forms
 Ligases - Formation of COC, COS, COO, and CON bonds by condensation reactions coupled to
ATP cleavage

1.1.3 State the properties of enzymes

 Almost all enzymes are proteins

 Enzymes accelerates the rate of reaction but are not consumed in overall process
 Exhibit high degree of specificity and stereo specificity for their substrates and type reaction
they catalyze.
 Catalysis involves the formation of the intermediate complex between the enzyme and the
substrate
 The region of the enzyme where the substrate binds is the active site

1.1.4 Explain the factors affecting rate of enzyme-catalyzed reactions

 Temperature- Increase in temperature increases the energy of the molecules thus having the
sufficient energy to overcome the energy barrier (activation energy). However, further increase
Module 1B SGD Session 1: Cell Bioenergetics

in temperature may induce denaturation of enzymes and will result to a decreases in rate of
reaction
 Substrate/Reactant concentration- The rate of reaction is the number of substrate molecules
converted to product per unit time. The rate of enzyme-catalyzed reaction increases with
substrate concentration until a maximal velocity is reached. (Vmax is the saturation of all
binding sites on the enzyme molecules present)
 Hydrogen Ion concentration (pH)- Extreme pH can also denature enzymes. The optimum pH
varies for different enzymes example pepsin, a digestive enzyme which is activated at pH 2
while other enzymes designed to work at neutral pH ill bee denatured by acidic environment
 Inhibitor- Inhibitor may compete for binding sites and may change the conformation of the
enzyme leading to inhibition of enzymatic activity

1.1.5 Describe/Explain the Michaelis-Menten equation and the Hill equation

1.1.6 Identify/Explain the types of enzyme inhibition

1.1.7 Identify common enzymes used in clinincal diagnosis

1.2 Identify and describe the three major sources of high energy phosphate that take part in
energy conservation or energy capture, to include:
1.2.1 Glycolysis
1.2.1.1 Identify the steps, precursors, enzymes and co factors involved
1.2.1.2 Identify significant immediate product
1.2.1.3 Identify inhibitors
1.2.2 Kreb’s Cycle
1.2.2.1 Identify the steps, precursors, enzymes and co factors involved
1.2.2.2 Identify significant immediate product
1.2.2.3 Identify inhibitors
1.2.3 Oxidative Phosphorylation
1.2.3.1 Identify description f respiratory chain, electron transfer, redox pairs
1.2.3.2 Identify descriptions of standard reduction potential and its importance
1.2.3.3 Describe the chemiosmotic model of oxidative phosphorylation
1.2.3.4 Identify the four major groups of inhibitors of mitochondrial ATP synthesis and
their examples.