Glycolysis and TCA cycle Quiz

Quiz #4/5
#4: Glycolysis (Fri, Feb 13th)
#5: TCA cycle (Thurs, Feb 26th)
Quiz will have the entire pathway:
All cofactors will be present
Most intermediate and enzymes removed
You fill in the missing names

Abbreviations are NOT acceptable answers

Draw the structure for 1 intermediate
Indicated by a larger box

Enzyme Regulation
Learning Objectives:
Understand how different conditions affect
enzyme activity.
Know the types of genetic control.
Describe how covalent modifications of enzymes
affect activity

Describe how non-covalent modifications of

enzymes affect activity.
Explain how covalent and non-covalent
modifications can be combined to regulate
enzyme activity.

Conditions Affecting
Enzyme Activity
pH
temperature

pH:
Enzymes have an optimum pH, based on:
required ionization state of amino acids

Effects of pH on Enzyme Activity

Protonation state of side chains
Variation in protein structure

Substrate binding
catalysis

Ionization of substrate
Substrate binding

Temperature
a

Protein
unfolding

Relative
Activity

Temperature

Control of Enzyme Activity

In response to overall needs of the cell or organism.
Modulate:
Enzyme Availability (Amount)
Enzyme Catalytic Activity

Control of Enzyme Availability

Balance rate of production with rate of degradation
Control of Gene Expression: rate of production
Constitutive Enzymes:
e.g. glycolytic enzymes
Inducible Enzymes:
e.g. -galactosidase
Repressible Enzymes:
e.g. enzymes of Cholesterol biosynthesis

Control of Proteolysis: rate of degradation

based on targeting to proteosomes (ubiquitin)

Regulation of
Enzyme Catalytic Activity

Modification of protein structure leads to

modification of protein activity
Covalent Modification
Irreversible
Reversible

Non-Covalent Modification
Allosteric regulators

Irreversible Covalent Modification:

Cleavage of peptide bonds
Inihibition (Proteolysis)
Proteosomes (ubiquitin)

Activation
H2O
+

"Inactive"

"Active"

Zymogen
Inactive precursor protein
Pancreas

Small
Intestine

Reversible Covalent Modification:

Modification of amino acid side chains

Protein Modification
(Phosphorylation/Dephosphorylation)

Page 390

Non-covalent Modification
(Allosteric regulators)
Effectors or Ligands
Positive: activators
Negative: inhibitors

Modification of protein structure changes

active site structure, affecting:
Substrate Binding
Catalytic rate
Both

Negative Effectors (Inhibitors)

+

Active
Site

I
I

Regulatory
Site

"inactive"
or
less active

"active"

Positive Effectors (Activators)

+

+
+

"inactive"
or
poorly active

"active"
or
more active

Glycogen Phosphorylase

Figure 12-16

Enzyme activity in cells is controlled by which of

the following?
I. modulation of protein degradation rates
II. modulation of protein expression levels
III. covalent modifications
IV. allosteric effectors

A) I, II
B) II
C) III
D) III, IV
E) I, II, III, IV

How might the (reversible) attachment of an inorganic

phosphate group to a hydroxyl-containing amino acid
side chain (Ser or Tyr) alter the activity of an enzyme?
A.

The phosphate group blocks the active site and prevents the
substrate from binding.

B.

Addition of the phosphate group changes the shape of the

enzyme.

C.

The binding affinity of the substrate is lowered because of

electrostatic repulsion.

D.

Addition of the phosphate group causes the enzyme to

dissociate into its separate subunits which are all in the R
state.