• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/21

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

21 Cards in this Set

  • Front
  • Back
What are oxidoreductases?
EC # 1; Enzymes that are involved in oxidation-reduction reactions. Use coenzymes such as NAD+, NADP+, FAD coenzyme Q, or O2 as the electron receptor; Examples include: Dehydrogenases, Oxidases, Reductases
Transferases
EC#2 : Enzymes that are involved in the Transfer of a chemical group (amino group, phosphoryl group, glycosyl
group, carboxyl group, etc.) from a donor to an acceptor (e.g., transaminases, kinases).
What kind of enzyme would I use for the following recation:
X-P + Z -> X + Z-P
Transferases - Kinases
Hydrolases
EC #3; Hydrolytic cleavage of covalent bonds between carbon and some other atoms
(e.g., peptidases, proteases, phosphatases, glycosidases).
Lyases:
EC #4 Non-hydrolytic cleavage of covalent bonds between carbon and other atoms such
as carbon, sulfur, and nitrogen (e.g., decarboxylases, dehydratases, aldolase).
What is the difference between Hydrolases and Lyases?
Hydrolases uses water and Lyases does not
Isomerases:
EC # 5; Molecular rearrangement within a molecule without any change in
molecular formula (e.g., isomerases, epimerases, mutases).
What enzyme catagory would I use if i wanted to change an molecule from D to L conformation
I would use an isomerases which basically changes the moves functional groups around without actually changing the molecular makeup
Ligases:
EC # 6 Formation of covalent bonds between carbon and other atoms such as sulfur,
nitrogen, or oxygen). Frequently, use ATP or GTP as the energy source to carry out the
reaction (e.g., carboxylases, thiokinases).
What are the three main categories of the non-protein componets of an enzyme? Where they derived from?
Prosthetic groups, coenzymes, cofactors; they come from vitamins
What does the vitamin thiamin give us
Thiamin a B1 vitamin gives us thiamin pyrophosphate
What does Riboflavin gives us
FAD and FMN
Whats does Niacin (Nicotinic Acid)
NAD+ and NADP+
What does pantothenic Acid give us
Coenzyme A
What does pyridoxine give us
pyridoxal Phosphate
How does the active site form?
Basically, when the protein folds together some different AAs are brought in close proxmity of each other thus forming the active site.
What happens at equlibrium to the concentrations of P and S where S -> P
they are not necessarily equal but stable. so the velocity of the forward reaction becomes equal to the velocity of the reverse reaction
Do enzymes effect the amount of product?
No, they only effect the time it takes to get the product.; the equilibrium state is reached much faster in the presence of the enzymes.
Is the free energy changed by using an enzyme?>
no, the free energy is the same.
what is the relationship between Velocity, and Activatiion energy?
V = 1/ Eact
What are the 3 main features of the active site of an enzymes?
-occupies only a small part of the enzyme, clefts of the enzyme
-it is 3 - dimensional
-the substrates are bound
weakly to the active site.they bind in a way that resembles thhe geometry of the transition state; the enzyme provides groups that enhance the probabilty that the transition state will occur.