L.2 Enzymes Flashcards
2.1 -2.2 BIOCHEM 3.1 BIOCHEM
Lucky 7 to be ALIVE Functions of ENZYMES?
- Lower Activation Energy
- Increase the Rate of Reaction
- Are pH & Temperature Sensitive
- Each Enzyme is Specific for Each Reaction
- Not Changed or Consumed by Reaction
- Do not Affect the overall change of G (Gibbs Free Energy)
- Do no Alter Equilibrium Constant
What are the 6 types of Enzymes?
- Lyases
- Isomerase
- Ligases
- Hydrolase
- Oxidoreductase
- Transferase
What is the difference between Lyases and Ligases?
Lyases, cut a single molecule into two molecules
“synthase” is the reverse
Ligases Catalyzed Addition or synthesis of reactions, bringing together large molecules that often require ATP
What do Isomerases do?
& what kind of other enzymes can they act/be like?
Isomerases rearrange bonds within a molecule, they can be oxidoreductases, transferases of lyases.
Catalyze reactions between stereoisomers
and constitutional isomers
How to Hydrolases work?
Hydrolases catalyze breaking molecules into two
by the addition of WATER.
Phosphatase; breaks molecule by cleaving phosphate…
…Peptidase
…Nuclease
…Lipases
What is the difference between Oxidoreductase and Transferase?
Oxidoreductase catalyzes the transfer of electrons between molecules,
they have cofactors such as NAD+ and NADP +
(Dehydrogenase, Reductase, Oxidase)
Transferase, Transfers or moves functional groups from one molecule to the other or within the same molecule.
- Aminotransferase*
- Kinases*
Delta G and Energy input/output on Enzyme Kinetics?
Endergonic Reactions require an Energy input and
delta G is GREATER than zero
Exergonic reactions release energy and
delta G is LESS than Zero
What can enzymes do provide favorable microenvironments?
- Alter charge
- Change pH
- Stabalization of transition states
- Bring reactive groups together
What is the difference between the lock and key
and the induced fit model?
The substrate and the enzyme fit like a
lock and key with set shapes,
in the induced fit model they are both different shapes
and then conform to a different shape when they come together.
What is the difference between cofactors and coenzymes?
Cofactors are inorganic molecule, like metal ions that can be ingested as diatary minerals, magnesiums.. calcium..ect.
- Coenzymes and Prosthetic groups are the two types of cofactors
- Aid in the function of enzyme
Coenzymes are small organic carrier molecules; groups like vitams or their derrivatives. NADH acts as electron carrier.
(NAD+,FAD, Coenzyme A)
- Assist in biological transformations
- easily removable
- a type of cofactor
The difference between Apoenzymes, Holoenzymes and Prosthetic groups
Apoenzymes are ezymes with out their cofactors
Holoenzymes are enzymes with cofactors; attached by covalent bonds
Prosthetic Groups are tightly bound cofactors or coenzymes that are necessary for enzyme function
Wernicke-Korsakoff Syndrome
The cause of excess alcohol consumption and/or poor diet
Thiamine Deficiency (VIT B)
Neurological Deficits
Delirium
Balance
No new memories
Wernicke-Korsakoff syndrome (WKS) is a neurological disorder. Wernicke’s encephalopathy and Korsakoff’s psychosis are the acute and chronic phases, respectively, of the same disease.
WKS is caused by a deficiency in the B vitamin thiamine. Thiamine plays a role in metabolizing glucose to produce energy for the brain. An absence of thiamine results in an inadequate supply of energy to the brain, particularly to the hypothalamus, which regulates body temperature, growth, and appetite, and also has a role in emotional response. The hypothalamus also controls pituitary functions, including metabolism and hormones, and mammillary bodies, where neural pathways connect various parts of the brain involved in memory functions. The disease is typically associated with chronic alcoholism, but may be associated with malnutrition or other conditions that cause nutritional deficiencies.
Name the 8 types of Vitamin B
- B1 THIAMINE
- B2 RIBOFLAVIN
- B3 NIACIN (NAD)
- B5 PANTOTHENIC ACID (CoA)
- B6 PYRIDOXAL PHOSPHATE
- B7 BIOTIN
- B9 FOLIC ACID
- B12 CYANOCOBALAMIN
How does carbon dioxide leave tissues?
Carbon Dioxide from the tissues combines with water with the help of
CARBONIC ANHYDRASE it is turned into
CARBONIC ACID
wich dissociates quickyly into Bicarbonate HCO3-
and H+ hydronium ion in the blood cell the
BICARBONATE
then leaves the RBC and enters the lungs along with Cl-
HCO3- + H+
leaves the lungs with chloride shuttle as
CO2 and Water
What are the 6 different types of functions of Proteins?
- Enzymes (enzymatic)
- Structural
- Motor
- Binding
- Cell Adhesion Molecules CAM’s
- Immunoglobins
What are 5 Characteristics of Actin?
- Makes up Microfilaments (thin filaments)
- Makes up thin Filaments in Myofibrils
- Most abundant in eukaryotic cells
- Have a positive and negative side
- Motor proteins can travel unidirectionally along actin filament
- (one-way street)
a protein that forms (together with myosin) the contractile filaments of muscle cell
What is Tubulin?
- Makes up Microtubules, microtubules then..
- providing structure
- chromosome separation in mitosis and meiosis
- Intracellular transport with KENESIN & DYEIN
- Has polarity
- Negative end located adjacent to the nucleus
- Positive in the periphery of the cell
The Function Of Microtubules. Microtubules are hollow, fibrous shafts whose main function is to help support and give shape to the cell. They also serve a transportation function, as they are the routes upon which organelles move through the cell.
What are the 3 Motor Proteins?
- Myosin
- Kinesins
- Dyneins
What is Myosin & how does it work?
- Myosin is the Primary Motor Protein that interacts with Actin.
- The THICK FILAMENT in a Myofibril
- Each subunit has a single head and neck
- Movement at the neck = power stroke of sarcomere contraction
- Cellular Transport
When an antibody or Ig binds to an antigen, what 3 things can occur?
- Neutralizing the antigen, making thr pathogen unable to exert its eefect on the body.
- Marking the pathogen for distruction by other white blood cells immediately; this marking function is called OPSONIZATION.
- Clupping together (AGGLUTINATING) the antigen anf antibosy into large insoluble protein complexes that can be phagocytized and digested by macrophages.
