Ques -: Describe the chemistry of two types of enzymes and explain how the apoenzyme forms ?
Ans ) Enzymes are also known as biological catalyst that increase the rate of reaction.
Most of the enzymes are proteins . It is act as synthesize reactions, or help in the chemical
breakdown .
If we talk about their types then ,
Based on the involvement in the sequence of amino acids that points out the structure that result in
demonstrating the enzyme's catalytic activity they are mainly of two types -:
Isomerase & ligase .
• Isomerase -: it includes the example of phosphoglucomutase that catalyzes the isomer formation.
Its chemistry
- During respiration ( internal) ,in the process of glycolysis there will be a conversion of glucose -
1- phosphate to glucose 6 phosphate.
• Ligase – it includes the example of Aldolase.
Its chemistry
- Ligase enzymes breaks the bond without catalysis by their catalytic activity.
- It increases the breakdown of fructose 1 ,6 phosphate to glyceraldehyde 3 phosphate.
APOENZYME & HOW IT IS FORMED?
• Apoenzyme is the inactive protein part that are composed of a series of amino acid.
• As they are responsible for enzyme substrate specificity (ES). Hence, it is important for enzymatic
activity.
• Apoenzyme ( a protein which is inactive) & non protein part of cofactor ( coenzyme) together form a
holoenzyme ( a conjugate enzyme) which is active.
Apoenzyme is formed due to the polypeptide chain in its chemical constituent and lack of non-protein
moiety.
Explanation -: The apoenzyme has a complex molecular structure . There is a formation of disulfide
bonds and other forms of bonds allows the primary, secondary, and tertiary structures to fold
automatically and gain stability.
Ans ) Enzymes are also known as biological catalyst that increase the rate of reaction.
Most of the enzymes are proteins . It is act as synthesize reactions, or help in the chemical
breakdown .
If we talk about their types then ,
Based on the involvement in the sequence of amino acids that points out the structure that result in
demonstrating the enzyme's catalytic activity they are mainly of two types -:
Isomerase & ligase .
• Isomerase -: it includes the example of phosphoglucomutase that catalyzes the isomer formation.
Its chemistry
- During respiration ( internal) ,in the process of glycolysis there will be a conversion of glucose -
1- phosphate to glucose 6 phosphate.
• Ligase – it includes the example of Aldolase.
Its chemistry
- Ligase enzymes breaks the bond without catalysis by their catalytic activity.
- It increases the breakdown of fructose 1 ,6 phosphate to glyceraldehyde 3 phosphate.
APOENZYME & HOW IT IS FORMED?
• Apoenzyme is the inactive protein part that are composed of a series of amino acid.
• As they are responsible for enzyme substrate specificity (ES). Hence, it is important for enzymatic
activity.
• Apoenzyme ( a protein which is inactive) & non protein part of cofactor ( coenzyme) together form a
holoenzyme ( a conjugate enzyme) which is active.
Apoenzyme is formed due to the polypeptide chain in its chemical constituent and lack of non-protein
moiety.
Explanation -: The apoenzyme has a complex molecular structure . There is a formation of disulfide
bonds and other forms of bonds allows the primary, secondary, and tertiary structures to fold
automatically and gain stability.
