Energy and Enzymes:: Lecture Presentation by Cindy S. Malone, PHD

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8

Energy and
Enzymes:

Part 2

Lecture Presentation by
Cindy S. Malone, PhD,
California State University Northridge

© 2017 Pearson Education, Inc.


How Enzymes Work
• Most biological chemical reactions occur fast
enough only in the presence of an enzyme
• Enzymes are protein catalysts
• Bring reactants together in precise orientations
• Make reactions more likely
• Are specific for a single type of reaction

© 2017 Pearson Education, Inc.


Enzymes Help Reactions Clear Two Hurdles

• Before a reaction can take place, reactants need to


1. Collide in a precise orientation (Active Site Binding)
2. Have enough kinetic energy to overcome repulsion
between electrons that come into contact as a bond
forms (Activation Energy)

© 2017 Pearson Education, Inc.


Enzymes Bring Substrates Together
• Substrates bind to the enzyme’s active site
• Substrates bind via hydrogen bonding or other
interactions with amino acid residues in the
active site
• Many enzymes undergo a conformational change
when substrates bind – induced fit

© 2017 Pearson Education, Inc.


Enzymes Bring Substrates Together
• An unstable intermediate condition called the
transition state is formed
• Activation energy (Ea) is required to strain
substrates’ bonds so they can reach the transition
state

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Enzymes Lower the Activation Energy
• Interactions between the enzyme and the substrate
• Stabilize the transition state
• Lower the activation energy required for the reaction
to proceed
• Enzymes are not consumed during the reaction

© 2017 Pearson Education, Inc.


Enzymes Lower the Activation Energy
• Enzyme catalysis has three steps:
1. I​nitiation—substrates are
precisely oriented as they bind to
the active site
2. T
​ ransition state facilitation—
interactions between the substrate
and active site R-groups lower the
activation energy
3. T
​ ermination—reaction products
are released from the enzyme

© 2017 Pearson Education, Inc.


Do Enzymes Work Alone?

• Many enzymes are regulated by molecules that are


not part of the enzyme itself:
1. C
​ ofactors are inorganic ions, such as Zn2+, Mg2+,
and Fe2+, that reversibly interact with enzymes
2. C
​ oenzymes are organic molecules, such as NADH
or FADH2, that interact with enzymes

3. P
​ rosthetic groups are non-amino acid atoms or
molecules that are permanently attached to proteins

© 2017 Pearson Education, Inc.


What Factors Affect Enzyme Function?

• An enzyme’s structure is critical to its function


• Protein structure is dependent on folding
• Enzyme function is dependent on certain
conditions
• Temperature affects the folding and movement of the
enzyme and its substrates
• pH affects the enzyme’s shape and reactivity
• Each enzyme has optimal temperature and pH

© 2017 Pearson Education, Inc.


Most Enzymes Are Regulated

• Regulatory molecules may control when and where


an enzyme functions
• Noncovalent Regulation – reversible (on and off
switch) – doesn’t change protein structure
• Covalent Regulation – Phosphorylation and Primary
Protein Structure change
• May either activate or inactivate the enzyme’s
function

© 2017 Pearson Education, Inc.


Regulating Enzymes via Noncovalent Interactions
• Regulation via noncovalent
interactions
• Competitive inhibition occurs when
a molecule competes with the
substrate for the active site
• Allosteric regulation occurs when a
molecule binds at a location other
than the active site
• Causes a change in enzyme
shape
• Can activate or deactivate the
enzyme

© 2017 Pearson Education, Inc.


Regulating Enzymes via Covalent Modifications
• Changes the enzyme’s primary
structure
• Can be reversible or irreversible
• Irreversible changes often result
from cleavage of peptide bonds
• Most common reversible
modification of enzymes is the
addition of phosphate groups
(phosphorylation)
• Causes a change in shape
• May activate or inactivate the
enzyme

© 2017 Pearson Education, Inc.


Enzymes Can Work Together in Metabolic
Pathways
• Metabolic pathways
• A series of reactions
• Each catalyzed by a different enzyme
• To build biological molecules

A -------------
enzyme 1 B --------------
enzyme 2 C -------------
enzyme 3 D

© 2017 Pearson Education, Inc.


Metabolic Pathways Are Regulated
• Feedback inhibition occurs
• When an enzyme in a
pathway is inhibited
(switched off) when
adequate amounts of the
final product are produced
• Pathway can shut down
when
• Products are no longer
needed by the cell

© 2017 Pearson Education, Inc.


Metabolic Pathways Evolve

• Metabolic pathways are vital to all cells


• Catabolic pathways break down molecules
• Anabolic pathways synthesize molecules

© 2017 Pearson Education, Inc.

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