Lecture Chp. 4: Cellular Metabolism Flashcards
All chemical reactions that occur in the body
Metabolic Processes
Two types of metabolic reactions
- Anabolism
2. Catabolism
Large molecules are made from small molecules (requires energy)
Anabolism
Larger molecules are broken down into smaller ones (releases energy)
Catabolism
Anabolism provides the materials needed for _____.
cellular growth and repair
Type of anabolic process
Dehydration Synthesis
Used to make polysaccharides, triglycerides, and proteins (produces water)
Dehydration Synthesis (Anabolism)
A catabolic process
Hydrolysis
Used to decompose carbohydrates, lipids, and proteins. Water is used to split the substances.
Hydrolysis
*Reverse of dehydration synthesis
Force water into the molecule to break it down
Hydrolysis
Type of reaction that releases energy
Exergonic
type of reaction that requires an input of energy
Endergonic
When you break a phosphate bond, you ____ energy
gain
the ability to do work
energy
energy stored
potential energy
energy of motion and heat
kinetic energy
Fast moving particles exhibit the energy heat
kinetic energy
- Help link endergonic and exergonic reactions
- are usually proteins
- speed up chemical reactions
enzyme
*act as a catalyst. ATP will eventually fall apart, but we can’t wait forever. So, we have enzymes b/c we need energy now!
The energy required to start a process
activation energy
Only _____ reactions are spontaneous
exergonic
Catalysts do _____
catalysis
How to catalysts increase the chances that a exergonic reaction will take place?
They manipulate chemical bonds so less activation energy is needed to start the process
Enzymes are biological _____ that bind to _____
biological catalysts; bind to substrates
Enzymes have a highly specific ______
active site
Enzymes bind to substrates through:
weak, non-covalent bons
When enzymes bind to substrates, what may happen?
Binding might change the shape of the enzyme temporarily
*induced fit
Depending on the temperature, an enzyme may bind to, alter, and release _____ molecules per second.
100,000
Composed of several non-covalently bonded enzymes
Multienzyme Complexes
Multicomplex enzymes:
rapidly accomplish a series of reactions
Most metabolic pathways:
- multiple steps
2. must be catalyzed by multiple enzymes
Aid enzymes in catalysis
cofactors
organic, non-protein molecules that aid enzymes in catalysis
Coenzymes (cofactor)
Reactions that move pairs of electrons
oxidation-reduction reactions
_____ will aid in oxidation-reduction reactions
cofactors
What is the most important coenzyme
Nicotinamide adenine dinucleotide (NAD+)
*know dinucleotide
What makes up NAD+
- AMP
- nicotinamide monophosphate
When NAD+ becomes reduced:
- it picks up 2 electrons in association with it
- creases NADH
NADH will donate the electrons it gained when NAD+ was reduced to another molecule, including:
those that make ATP
NAD+ =
oxidized
NADH =
reduced
Molecules are ____ when they lose electrons
Oxidized
*oxidation reactions
Molecules are ____ when they gain electrons (become more negative)
Reduced
*Reduction reactions
When enzymes fall apart
denatured
Increasing ambient temperatures:
-increases the rate of enzymatic work up to a point (extreme temperatures may denature the protein)
All enzymes have an ______ temperature
optimum
pH can determine:
the efficiency of enzymes
Optimum pH for most proteins is between a pH of:
6 and 8
What is the exception for an enzyme that has a very acidic pH
pepsin (stomach acid)= ph of 2
Any molecule that changes the activity of an enzyme is an _____
effector
*could increase or decrease
effectors that inhibit enzyme activity are:
inhibitors
Molecules that resemble a substrate and can occupy an active site are:
steric inhibitors
competitive inhibitors
steric inhibitors
Get food from something else (another organism)
heterotrophs
synthesize own organic molecules to obtain energy
autotrophs
All chemical reactions that occur in the body
metabolism
what is an example of a steric inhibitor?
carbon monoxide
*Binds to hemoglobin and prevents hemoglobin from picking up oxygen
Noncompetitive inhibitors bind somewhere on the enzyme other than the _____
active site
non-competitive inhibitor is also known as an
allosteric effector
A noncompetitive inhibitor changes the ____
shape of the active site
When can ATP function as an allosteric effector?
with PFK
*ATP can bind to PFK so that cells can’t break down Glucose