Enzymes,

Neurotransmitters,
and Hormones
BIOCHEMISTRY LECTURE
MC 101

Prepared by:
MBCA Cepillo
OUTLINE

ENZYMES NEUROTRANSMITTERS
01 02

HORMONES SUMMARY
03 04 Enzymes, neurotransmitters,
and hormones
 OBJECTIVES
At the end of the lesson, the student must be able to:

1. Identify the different types and classes of enzymes;

2. Define enzyme related terms such as cofactors,
coenzymes, holoenzyme, etc. ;
3. Illustrate the models of enzyme action;
4. List the varying enzyme specificity;
5. Discuss the factors that affect enzyme activity; and,
6. Explain enzyme regulation.
INTRODUCTION
 METABOLISM

● Consists of a series of reactions that

occur within cells of living organisms
to sustain life

● defined as the total amount of

biochemical reactions in a biological
organism that maintain the healthy
operation of cells

● provides the energy necessary for

biological processes
01

ENZYMES
 ENZYMES

● Biocatalyst

● All enzymes are proteins, except

ribozymes

● Highly specialized catalysts with

extraordinary catalytic power and
also with remarkable specificity

● Known as the basis of life since

they catalyse almost all cellular
reactions
ENZYMES
 ENZYMES

● Catalyze the rate of biochemical reactions occurring in various life

processes

● Do not undergo any chemical change but are regenerated at the end of the
rxn

● SUBSTRATES: substances on which enzymes act to yield products

 ACTIVE SITE

● where the enzyme combines with the

substrate and transforms the substrate to
product

● where the catalytic action happens

● ‘catalytic’ or ‘active’ amino acids or ‘catalytic

residues’
○ Amino acid residues present in the active
sites that leads to catalytic action
○ Promotes the formation or degradation of
bonds
 ENZYMES

ENDOENZYMES EXOENZYMES

● Synthesized within the cell ● Secreted from the cells into

→ intracellular the environment
● Most enzymes are → extracellular
endoenzymes ● Break down large food
● Can be found in the molecules or harmful
cytoplasm, nucleus, and chemicals
mitochondria ● Ex: cellulase, amylase,
● Ex: proteases, lipases penicillinase
 ENZYMES

CONSTITUTIVE REGULATED

● Always present ● Not constantly present

● Always produced in equal ● Production is turned on

amounts or at equal rates, (induced) or turned off
regardless of the amount of (repressed) in response to
substrate changes in the [substrate]

● Ex: enzymes involved in ● Ex: Lac operon

glucose metabolism
(glucokinase and hexokinase)
 ENZYMES

SIMPLE CONJUGATED
● Contains a non-protein group
called a cofactor
→ required for biological activity

● Consists entirely of protein ● APOENZYME: simple enzyme

produced when the cofactor of a
(amino acid chains)
conjugated enzyme is removed
→ generally biologically inactive
● Ex: trypsin, pepsin, and
urease ● HOLOENZYME: complete and
biologically active conjugated
enzyme
→ simple enzyme (apoenzyme) +
cofactor
 COFACTOR

● Nonprotein components of an
enzyme

● Can be linked to the protein

portion of the enzyme either
covalently or noncovalently

● ESSENTIAL ION = inorganic

cofactor

● COENZYME = organic cofactor

 COENZYMES

● Some cofactors are simple metal

ions and others are complex
organic groups (coenzymes)

● COSUBSTRATE: cofactor that is

required in fixed quantity for
reaction to occur

● PROSTHETIC GROUP: cofactors

tightly associated with the protein
covalently or noncovalently
MODELS OF ENZYME
ACTION
 1. LOCK AND KEY

● Proposed by Emil Fischer in 1894

● Involves the complementarity between

the shapes of the enzyme and the
substrate

● States that the substrate fits perfectly

into the enzyme
○ Like a lock (enzyme) and key
(substrate) would

● The enzyme and substrate shape do

not influence each other.
 1. LOCK AND KEY
● Disadvantages
○ does not explain the stabilization of the intermediate shape of the
substrate
○ Unable to describe multiple substrate binding to an enzyme
○ States that enzyme is a rigid structure → not acc to recent
research
 2. INDUCED FIT
● Proposed by Daniel Koshland in 1958

● resemble the fitting of a hand into a glove

○ Enzyme (glove) and substrate (hand)

● The binding of the substrate induces a conformational change in the active

site of the enzyme
○ The enzyme may distort the substrate forcing it into a conformation
similar to that of the transition state
 2. INDUCED FIT

● Disadvantage
○ the pathway requires the formation of a Enzyme-substrate
complex 1 which is not favourable thermodynamically
SPECIFICITY OF
ENZYMES
 ENZYME SPECIFICITY

1. Absolute specificity
● Enzyme will catalyze only one reaction

2. Group specificity
● Enzyme will act only on molecules that have specific functional
groups such as amino, phosphate, and methyl groups

3. Linkage specificity
● Enzyme will act on a particular type of chemical bond regardless
of the rest of the molecular structure

4. Stereochemical specificity
● enzyme will act on a particular steric or optical isomer
 NAMING AND
CLASSIFYING ENZYMES
FACTORS THAT AFFECT
ENZYME ACTIVITY
 Substrate Concentration

● ↑ [substrate] = ↑ rate of enzyme activity

○ rate of enzyme activity only
increases up to a certain value

● enzymes become saturated

● not enough enzyme molecules available

to break down the excess substrate
molecules
METAL IONS
ENZYME REGULATION
 ENZYME REGULATION
● Metabolic pathways

DIRECT CONTROL
● Quickest way to regulate
● Competitive and non-competitive
inhibition

GENETIC CONTROL
● Slower because ‘switch’ is
mediated by accumulation or
production of product
○ Induction and Repression
 ENZYME REGULATION
GENETIC CONTROL
● More long term effects

● REPRESSION
○ Excess of the end product binds to
the genetic component and turns it
‘off’

● INDUCTION
○ Induced by the presence of substrate
○ Binds to the genetic component and
turns it ‘on’
○ Make enzymes necessary for action
 IRREVERSIBLE INHIBITION

● inactivates an enzyme by
bonding covalently to a
particular group at the active
site

● cannot be reversed by the

addition of excess substrate
 REVERSIBLE INHIBITORS

Regulatory Molecules
● Activator and inhibitor

Cofactors
● Many enzymes are only active
when bound to cofactors

Compartmentalization
● Storing enzymes

Feedback inhibition
● Inhibited by the end product
FEEDBACK INHIBITION
CELL SIGNALING
 CELL SIGNALING
Intercellular signaling Intracellular signaling
● Communication between cells ● Communication within a cell
● ‘Inter’ = between ● ‘Intra’ = inside
 AUTOCRINE

● A cell targets itself

○ Auto = ‘self’
● Often occurs with other types of
signaling

● During early development of an

organism

● Regulates pain sensation and

inflammatory responses

● Programmed cell death

 PARACRINE

● Signals that act locally between cells that are

close together

● Paracrine signals move by diffusion through

the extracellular matrix

● Usually elicit quick responses

● paracrine ligands are usually quickly degraded

by enzymes or removed by neighboring cells

● NEUROTRANSMITTERS
 ENDOCRINE
● Signals from distant cells
○ Originate from endocrine cells

● Usually produce a slower response but have a longer lasting effect

● HORMONES
○ ligands released in endocrine signaling
 DIRECT
● GAP JUNCTIONS: connections between plasma membranes of
neighboring cells
○ Water-filled channels allowing small signaling molecules to diffuse
between cells
● Ex: Ca2+
● Specificity of the channels ensures that the cells remain independent but
can quickly and easily transmit signals
SUMMARY
 ENZYMES
● Involved in metabolic processes

● Highly specialized biocatalysts with extraordinary catalytic power and

also with remarkable specificity
ENZYMES
MODELS OF ENZYME ACTION
 SPECIFICITY

ENZYME SPECIFICITY

1. Absolute
2. Group
3. Linkage
4. Stereochemical
ENZYME CLASSIFICATION
 ENZYME REGULATION

● DIRECT CONTROL
○ Competitive
○ Noncompetitive
● GENETIC CONTROL
○ Induction
○ Repression

● IRREVERSIBLE vs REVERSIBLE INHIBITION

○ Reversible inhibition
■ Competitive vs. Noncompetitive

● Feedback Inhibition
 CELL
SIGNALING
 REFERENCES
● Nelson, David L., Cox, Michael M. (2017). Lehninger Principles of Biochemistry. 7th Edition. W.U.Freeman and Co. Ltd
● Murray, RK., Bender, DA., Botham, KM., Kennelly, PJ., Rodwell, V.W., & PA Weil. (2009). Harper’s Illustrated biochemistry.
28th ed. US: McGraw-Hill Medical.
● Talaro, K.P. & B. Chess. (2012). Foundations in Microbiology. 8th ed. McGraw-Hill Companies, Inc.
● Khan Academy.(n.d.). Enzyme regulation. Retrieved 22 Sept 2022 from
https://www.khanacademy.org/science/ap-biology/cellular-energetics/environmental-impacts-on-enzyme-function/a/
enzyme-regulation
● Mattaini, K.R. (n.d.). Introduction to Molecular and Cell Biology: Cell Communication. Retrieved 22 Sept 2022 from
https://rwu.pressbooks.pub/bio103/chapter/cell-communication/
● UFSC. (n.d.). Introduction to Enzymes. Retrieved 23 Sept 2022 from
https://moodle.ufsc.br/pluginfile.php/4487489/mod_resource/content/1/Enzimas_fundamentos.pdf
● North Arizona University. (n.d.). Chapter 8: . Retrieved 23 Sept 2022 from
https://www2.nau.edu/~fpm/bio205/Sp-10/Chapter-08.pdf
● differencebetween.info. (n.d.). Difference between Cofactor and Coenzyme. Retrieved 23 Sept 2022 from
http://www.differencebetween.info/difference-between-cofactor-and-coenzyme
● Geeksforgeeks.org. (2022). Cofactors – Definition, Structure, Types, Example. Retrieved 24 Sept 2022 from
https://www.geeksforgeeks.org/cofactors-definition-structure-types-examples/
● Ebi.ac.uk. (2021). CHEBI:23357 - cofactor. Retrieved 24 Sept 2022 from
https://www.ebi.ac.uk/chebi/searchId.do?chebiId=23357#:~:text=Coenzymes%20are%20further%20divided%20into,tr
ansiently%20bound%20to%20the%20protein
● Sinha, R. (n.d.). Protein Biochemistry and Enzymology: Models for Enzyme Action. Retrieved 24 Sept 2022 from
http://biochem.du.ac.in/web/uploads/41%20Models%20for%20Enzyme%20Action.pdf
 REFERENCES
● Saylordotorg.github.io. (n.d.). Enzyme Action. Retrieved from
https://saylordotorg.github.io/text_the-basics-of-general-organic-and-biological-chemistry/s21-06-enzyme-action.html
● Judge, A. & M.S. Dodd. (2020). Metabolism. Essays Biochem. 2020 Oct; 64(4): 607–647. Published online 2020 Aug
24. doi: 10.1042/EBC20190041
● Differences Between Catabolism and Anabolism. Retrieved 24 Sept 2022 from
https://byjus.com/biology/differences-between-catabolism-and-anabolism/
● Ahmad Coaching. (2020). Lock and Key Model | Key Points and Limitations. Retrieved 24 Sept 2022 from
https://www.ahmadcoaching.com/2020/12/lock-and-key-model-of-enzyme.html#:~:text=Limitations%20of%20the%2
0lock%20and%20key%20model&text=This%20model%20does%20not%20explain,not%20supported%20by%20recent%
20research
● Carr, S. (2009). Induced-Fit Model of enzyme catalysis. Retrieved 24 Sept 2022 from
https://www.mun.ca/biology/scarr/Induced-Fit_Model.html
● BBC. (2022). Enzymes. Retrieved 24 Sept 2022 from
https://www.bbc.co.uk/bitesize/guides/zwxv6yc/revision/2#:~:text=Enzymes%20will%20work%20best%20if,activity%
20does%20not%20increase%20forever
● Ahern, K. % I. Rajagopal. Enzyme Inhibition. Retrieved 24 Sept 2022 from
https://chem.libretexts.org/Courses/University_of_Arkansas_Little_Rock/CHEM_4320_5320%3A_Biochemistry_1/05%
3A_Michaelis-Menten_Enzyme_Kinetics/5.4%3A_Enzyme_Inhibition
● Davey, R. (2022). The Biochemistry of Metabolism. Retrieved from
https://www.news-medical.net/life-sciences/The-Biochemistry-of-Metabolism.aspx#:~:text=Metabolism%20can%20b
e%20defined%20as,maintaining%20the%20structure%20of%20organisms
● Cherry, K. (2022). What are neurotransmitters? Retrieved 24 Sept 2022 from
https://www.verywellmind.com/what-is-a-neurotransmitter-2795394
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