Intro to Enzymology Flashcards
Are biological proteins that catalyze biochemical reactions. Intracellular proteins produced by living cells
Enzymes
T/F: Enzymes increase the rate or velocity of chemical reactions
TRUE
T/F: In the laboratory, enzymes are measured based on their activity and not by their absolute values
TRUE
Activity of the enzyme to a substrate is __ to their concentration
directly proportional
Majority of enzymes are located
Intracellular
If there’s an increase in plasma, it indicates:
- Cell is injured or damaged
- Increased membrane permeability
Functions of enzymes (6)
- Hydration of Carbon dioxide
- Nerve induction
- Muscle contraction
- Nutrient degradation
- Growth and reproduction
- Energy storage and use
A waterless cavity of an enzyme
where substrates bind and undergo a chemical reaction
Active site
Cavity other than the active site that binds regulatory or effector molecules
Allosteric site
T/F: Binding of the active site and substrate is SPECIFIC and must fit in order to bind with each other
TRUE
Substances acted upon by enzymes. It is specific for a particular enzyme
Substrate
Non-protein entities added in the enzyme-substrate complex to manifest enzyme activity.
Cofactors
What are the types of cofactors?
- Coenzyme
- Activator
- Isoenzymes
- Apoenzyme
- Holoenzyme
Also known as the second substrate, an organic cofactor that hastened or speed up enzymatic reactions
Coenzyme
Example of coenzyme
NAD and NADP
Metallic or nonmetallic ions that is added to enhance the enzyme activity. They alter the spatial configuration of enzyme active site to facilitate substrate binding
Activator
Example of Metallic activator
Mg, Ca, Zn, Fe
Example of Nonmetallic activator
Cl and Br
Enzymes with similar enzymatic activity but differ in physical, biochemical, and immunologic characteristics
Isoenzymes
T/F: In the lab, isoenzyme measurement is preferred than the Total enzyme activity measurement
TRUE
Example of isoenzyme
CK Isoenzymes
CK 1
CNS
CK 2
Myocardium
CK 3
Skeletal muscles and also found in the heart
Protein portion of the enzyme. When
this is subjected to the denaturation process, enzyme activity is lost
Apoenzyme
What structure is destroyed when there’s a denaturation reaction?
Tertiary structure
The process of heating at 56degC can lead to
Denaturation
Active substance formed by the combination of a coenzyme and apoenzyme (coenzyme + apoenzyme)
Holoenzyme
