ENZYMES

- macromolecules
- proteins, produced in living systems
- globular proteins with a specific tertiary shape
- specific to only one reaction
- help in breakdown, rearrangement, or synthesis reactions

CHARACTERISTICS:

A. Catalytic Power

- enzymes are biological catalysts or organic catalysts

- increase the rate of metabolic reactions and make biochemical reactions happen faster
- almost all biological reactions involve enzymes (RNAs are capable of catalyzing some reactions
- accelerate the rates of reactions by over a million-fold so reactions that would take years in the absence of catalyst can occur
in fractions of seconds if catalyzed by the appropriate enzyme.

Catalyst

- chemical involved, but not changed by a chemical reaction

- enzymes function as organic

B. Enzyme’s Specificity

Enzyme-substrate Specificity

- enzyme is specific for the substrate

- Substrate – reactant that binds to an enzyme
- Active Sites – very precise shapes, only one substrate can fit in each site and is chemically attracted to it

FUNCTIONS AND TYPE OF THE ENZYMES

Catabolic Enzymes – enzyme that break down their substrates

Anabolic Enzymes – build complex molecules from their substrates

Catalytic Enzymes – enzyme that affect the rate of reaction

A. Recommended Name:

- enzyme names have suffix “-ase” attached to the substrate of the reaction (urease)
- to description of the action performed (lactate dehydrogenase)
- some enzymes retain their original trivial names (trypsin and pepsin)

PARTS OF ENZYME:

1. Apoenzyme

- polypeptide or protein part of enzyme

- may be inactive in its original synthesized structure

Proenzyme or zymogen

- inactive form of apoenzyme

- removal of extra amino acids – allows the final specific tertiary structure to be formed before it is activated as apoenzyme

2. Cofactors

- non-protein substance
- Coenzyme – organic cofactor, derived from a vitamin
- Metal Ion Activator – inorganic metal ion cofactor
- Major reason for the nutritional requirement for minerals – to supply metal ions such as Zn, Mg, Mn, Fe, Cu, K, and Na for
use in enzymes as cofactors

Holoenzymes

- active enzyme with its non-protein component

FINAL ENZYME

- type of association between cofactor and apoenzyme varies:

- bonds – loose, come together only during the course of a reaction
- bonds – firmly bound together by covalent bonds

The Activating Role of Cofactor

- changing it geometric shape

- participating in the overall reaction
The binding of a cofactor to an apoenzyme – required to form an active holoenzyme

1. Apoenzyme becomes active – by binging of cofactor to enzyme

2. Holoenzyme formed when – cofactor binds to the enzyme’s active site

EXAMPLES OF ENZYMES:

Lactase – breaks down Lactose into Glucose and Galactose

Catalase – breaks down Hydrogen Peroxide into Water and Oxygen

Glycogen Synthase – catalyzes the formation of Glycosidic Bonds between Glucose molecules

ATP-ase – breaks down ATP into ADP, producing energy

ACTIVE SITE

- part of enzyme that acts a catalyst

- region on an enzyme that binds to a protein during reaction
- complementary to the substrate it catalyzes

SUBSTRATE

- one or more molecules upon which an enzyme act

REST OF ENZYME

- much larger
- involved in maintaining the specific shape of enzyme

REACTION INVOLVING ENZYME OCCURS

- substrate is turned into a product

Enzyme-substrate complex – formed when a substrate molecule interacts with the active site of an enzyme

After formation of enzyme-substrate complex – substrate molecule undergoes a chemical reaction and converted into a new product

HOW ENZYMES WORK

- by lowering the activation energy of a reaction

- by putting stress on the bonds or by holding molecules close together – this increases the likelihood of a reaction, and lowers
the energy required to begin it

Activation Energy – minimum energy required to cause a process to occur

LOCK-and-KEY MODEL

- model of how enzymes catalyze substrate reactions

- states that the shape of active sites of enzymes are complementary to the shape of substrate
- When substrate molecule collides with an enzyme – active shape if complementary, substrate will fit into the active site and
an enzyme-substrate complex will form
- The enzyme will catalyze the reaction, and the products, together with the enzyme, will form an Enzyme-Product Complex.
- it is possible for an enzyme to catalyze a reverse reaction.

INDUCED-FIT MODEL/HYPOTHESIS

- recent model, backed up by evidence, widely accepted as describing the way enzymes work
- states that shape of active sites are not complementary, but change shape in the presence of a specific substrate to become
complementary
- active site forms a complementary shape to the substrate after binding
- When substrate molecule collides with an enzyme – shape of enzyme’s active site will change so that the substrate fits and an
Enzyme-Substrate Complex can form
1. Substrate enters active site of enzyme
2. Enzyme-Substrate Complex forms (enzymes changes shape slightly as substrate bind)
3. Substrate is converted to products
4. Products leave the active site of enzyme
FACTORS AFFECTING ENZYME ACTIVITY

- environmental conditions
- changing these alter the rate of reaction cause by enzyme
- In nature, organisms adjust the conditions of their enzymes to produce an optimum rate of reaction, where necessary, or they
may have enzymes which are adapted to function well in extreme conditions where they live.

1. Temperature

- temperature increases, rate of reaction increases because of Kinetic Energy

- effect of bond breaking will become greater, rate of reaction will decrease
- Enzyme’s Optimum Temperature – temperature at which the maximum rate of reaction occurs
- Most enzymes in the human body have an Optimum Temperature of around 37.0 degrees

2. pH – Acidity and Basicity

- pH – measures the acidity and basicity of a solution

- measure of Hydrogen Ion concentration, good indicator of Hydroxide Ion concentration
- ranges from pH1 to pH14
- lower pH values, higher H and lower OH concentrations
- enzymes have optimum pH between 6 and 8
- Pepsin – optimum pH 1-2
- Alkaline Phosphate – optimum pH 9-10
- Acid Phosphate – optimum 4-5

SUBSTRATE CONCENTRATION

- increasing substrate concentration, increases rate of reaction (more substrate molecules will be colliding with enzyme
molecules, so more product will be formed
- However, after a certain concentration, any increase will have no effect on the rate of reaction, since Substrate Concentration
will no longer be the limiting factor. The enzymes will effectively become saturated, and will be working at their maximum
possible rate.

ENZYME CONCENTRATION

- increasing enzyme concentration will increase rate of reaction (more enzymes will be colliding with substrate molecules)
- However, this too will only have an effect up to a certain concentration, where the Enzyme Concentration is no longer the
limiting factor.

ENZYME INHIBITORS

Allosteric Interactions

- allow an enzyme to be temporarily inactivated.

- Binding of Allosteric Effector – changes shape of enzyme, inactivating it while the effector is still bound

Competitive Inhibition

- works by the competition of the regulatory compound and substrate for the binding site
- If enough regulatory compound molecules bind to enough enzymes, the pathway is shut down or at least slowed down.

OXIDATION-REDUCTION REACTION

Redox Enzymes – enzymes that catalyze the redox between two molecules

Oxidation-Reduction Reaction – any chemical reaction in which the oxidation number of a molecule, atom, or ion changes by gaining
or losing an electron.

Reduced half gains electrons - oxidation number decreases

Oxidized half loses electrons – oxidation number increases

OIL RIG – “oxidation is loss” & “reduction is gain”

LEO says GER – “loss of e =oxidation” & “gain of e = reduction”

Redox Reactions – vital to some of the basic functions of life

ENZYMATIC REDOX REACTIONS

Redox Reactions

- foundation of life
- reactions in which a substrate becomes more oxidized/ more reduced
- basis for energy used to support life

Redox Enzymes

- accelerate these reactions enough for them to be biologically useful to support life
- enzymes are needed to make redox reactions useful