Enzymes Reclec Flashcards
Act as biological catalyst
Enzymes
Increases the rate of reaction
Catalyst
Other term of inorganic cofactors of enzymes
Activators
Two cofactors of enzymes
Inorganic and organic
Other term for organic cofactors
Coenzymes
Enzymes that does not have a cofactor
Apoenzymes
Complete and active enzyme
Holoenzymes
Enzymes’ inactive form
Proenzyme / zymogen
Variants of enzymes
Isoenzymes
Where does the substrate binds to?
Active site
Where does the regulatory molecules binds?
Allosteric site
Who developed or established the classification system of enzymes
Enzymes commission (international union of biochemistry)
Enumerate the 6 classes of enzymes
1 oxidoreductases
2 tranferases
3 hydrolyses
4 lyases
5 isomerases
6 ligases
Joining of two molecules that needs ATP
Ligases
Redox reactions
Oxidoreductases
Transfer atom/groups
Tranferases
Removal of groups and creates double bond
Lyases
The binding of an enzymes to a substrate is a ______
Physical absorption
The substrate fits like a lock and the substrate binds exactly to the enzymes.
Lock & key theory
It imply that your enzymes are rigid
Lock & key theory
The active site of this theory undergo conformational change
Induced fit theory
The widely accepted theory
Induced fit theory
Dependent on substrate concentration
First - order kinetics
Dependent in enzyme concentration
Zero-order kinetics
One substrate will only bind to one enzymes
Absolute specificity
The enzyme will only accept substrate that has a hydrogen bond
Bond specificity
The enzyme will only accept the substrate that has the same group
Group specificity
The enzyme can only accept substrate that has the same configuration
Steroeoisometric specificity
6 factors affecting enzymes activity
1 enzyme /substrate concentration
2 pH
4 temperature
4 cofactors
5 inhibitors
6 interference
All enzymes are bound to substrate
Saturation kinetics
Optimal pH for most enzymes
7-8
Alkaline phosphatase requires a pH of _____
9-10
Acid phosphatase requires a pH of ___
5
Acid phosphatase requires a pH of ___
5
Optimal temperature of enzymes
37 degree Celsius
Loss of the folding structure of a protein
Denaturation
Inactivation of enzymes occurs at what temperature
60-65 deg.celsius
Temperature of denaturation of enzymes
40-50 deg. Celsius
Non-protein molecules necessary for enzyme activity
Cofactors
Inhibitors binds to active site
Competitive inhibitors
Inhibitors binds to other sites
Non-competitive inhibitor
Inhibitors binds to ES complex
Uncompetitive inhibitors
Substrate needed to achieve maximum velocity
Vmax
Substrate needed to catalyze a reaction
Km
Vmax remains but km increases
Competitive inhibition
Vmax decreases but Km remains
Non-competitive inhibition
Vmax and Km both decrease
Uncompetitive inhibition
Breakdown of RBCs
Hemolysis
Interference that increase the enzyme activity
Hemolyzed
Interference that decreases the enzyme activity
Lipemic
When or what phase do you measure your enzyme activity
Linear phase
Measurement of enzyme activity that stops
Fixed
Measurement of enzyme activity that has no ends or it is measured continuously
Continuous/kinetic
What do you use to measure the enzyme activity continuously
Continuous - reading spectrophotometer
