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Flashcards in L.2 Enzymes Deck (34)
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1

Lucky 7 to be ALIVE Functions of ENZYMES?

  1. Lower Activation Energy
  2. Increase the Rate of Reaction
  3. Are pH & Temperature Sensitive
  4. Each Enzyme is Specific for Each Reaction
  5. Not Changed or Consumed by Reaction
  6. Do not Affect the overall change of G (Gibbs Free Energy)
  7. Do no Alter Equilibrium Constant

2

What are the 6 types of Enzymes?

  1. Lyases 
  2. Isomerase
  3. Ligases
  4. Hydrolase
  5. Oxidoreductase
  6. Transferase

3

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

4

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

5

How to Hydrolases work?

Hydrolases catalyze breaking molecules into two

by the addition of WATER.

 

Phosphatase; breaks molecule by cleaving phosphate...

...Peptidase

...Nuclease

...Lipases 

6

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

 

7

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 

8

What can enzymes do provide favorable microenvironments?

 

  1. Alter charge
  2. Change pH
  3. Stabalization of transition states
  4. Bring reactive groups together

9

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.

10

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

11

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

12

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. 

13

Name the 8 types of Vitamin B

  1. B1 THIAMINE
  2. B2 RIBOFLAVIN
  3. B3 NIACIN (NAD)
  4. B5 PANTOTHENIC ACID (CoA)
  5. B6 PYRIDOXAL PHOSPHATE
  6. B7 BIOTIN
  7. B9 FOLIC ACID
  8. B12 CYANOCOBALAMIN

14

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

15

What are the 6 different types of functions of Proteins?

  1. Enzymes (enzymatic)
  2. Structural 
  3. Motor
  4. Binding
  5. Cell Adhesion Molecules CAM's
  6. Immunoglobins

16

What are the 5 types of Structural Proteins?

  1. Collagen
  2. Actin
  3. Tubulin
  4. Keratin
  5. Elastin

CAT-EK

17

What are 3 Characteristics of Collagen?

  1. Trihelical Fiber 
  2. Most of extracellular matrix of connective tissue
  3. Strenght and flexibility

Collagen is the most abundant protein in your body. It is the major component of connective tissues that make up several body parts, including tendons, ligaments, skin and muscles

18

What are 5 Characteristics of Actin? 

  1. Makes up Microfilaments (thin filaments)
  2. Makes up thin Filaments in Myofibrils
  3. Most abundant in eukaryotic cells
  4. Have a positive and negative side
  5. Motor proteins can travel unidirectionally along actin filament
  6. (one-way street)

a protein that forms (together with myosin) the contractile filaments of muscle cell

 

19

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.

20

What are 4 characteristics of Keratins?

  • Intermediate filament proteins in Epithelial Cells
  • Mechanical integrity of cell
  • Function as regulatory proteins
  • Hair and nails

21

What are 3 characteristics of Elastin?

  1. Extracellular Matrix of Connective Tissue
  2. Stretches and recoils like a spring and
  3. Restores the original shape of the tissue 

22

What are the 3 Motor Proteins?

  1. Myosin 
  2. Kinesins
  3. Dyneins

23

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

 

24

What are Kinesins & Dyneins?

Are the motor proteins associated with Microtubules

25

Explain how  Kinesins and Dyneins work in 3 key ideas.

 

 

  • Have Two Heads, one remaining attached to tubulin at all times
  • Kinesin; Aligns chromosomes during anaphase of mitosis
  • Dyneins; the Sliding movement of cilia and flagella 

 

Both for vesicle transport w/opposite polarities

Kinesin; towards + & Dyneins; towars -

26

What are Binding Proteins?

A binding protein is any protein that acts as an agent to bind

two or more molecules together.

 

Stabalizing functions in individual cells and body

do this by transporting or sequestering molecules by binding to them

27

What are three examples of binding proteins?

  1. Hemoglobin
  2. Calcium Binding Proteins
  3. DNA Binding Proteins

28

What are three characteristics of Cell-Adhesion Molecules (CAM)?

  1. Found on the Surface of most cells 
  2. Aid in Binding cells to the extracellular membrane or other cells
  3. They are Integral membrane proteins.

29

What are the 3 types of CAM's?

 

S I C

  1. Selectins
  2. Integrins
  3. Cadherins

 

30

What are 3 characteristics of Cadherins (CAM)?

  1. They are Glycoproteins
  2. They mediate Calcium dependent cell adhesion
  3. Hold epethelial cells together (or similar cells together)