Enzymes
Enzymes are biological molecules typically proteins that speed significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They are vital for life and serve as a wide range of important functions in the body, such as aiding in digestion and metabolism.
Some enzymes help break large molecules into smaller pieces that are more easily absorbed by the body. Other enzymes help bind two molecules together to produce a new molecule. Enzymes are highly selective catalysts, meaning that each enzyme only speeds up a specific reaction.
Enzymes are categorized based on the reaction they help catalyze. Examples of enzymes include:
- Amylase
- Proteinase
- Kinase
- Maltase
- Fructase etc.
What You Need To Know About Enzymes
- An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process.
- Enzymes are large molecules.
- Enzymes are mainly globular proteins.
- Enzymes act as biological catalysts.
- Enzymes’ structure remains unaltered throughout the reaction.
- Enzymes are very specific to the reaction they catalyze.
- Examples of enzymes include Amylase, protease, kinase, maltase, fructase etc.
Coenzymes
A coenzyme is a small organic molecule but not a peptide, that binds to an enzyme and whose presence is essential to the activity of the enzyme. It is considered to be an assistant molecule for biochemical reaction. Coenzymes provide a transfer site for a functioning enzyme in most cases. It often functions as an intermediate carrier of electrons, specific atoms or functional groups, allowing a reaction to occur.
Coenzymes are usually not part of an enzyme’s structure or the substrate of the reaction. The coenzyme may either be a prosthetic group-(a tightly bound coenzyme) or a co-substrate (a loosely bound small organic molecule). An inactive enzyme without the cofactor is referred to as an Apoenzyme whereas the complete enzyme with cofactor is referred to as a Holoenzyme.
Examples of coenzymes include:
- Nicotinamide adenine dinucleotide (NAD)
- Flavin adenine dinucleotide (FAD)
- Adenosine Diphosphate (ADP)
- Coenzyme A (CoA)
- Thiamine pyrophosphate (TPP)
- Pyridoxal phosphate (PLP)
- Tetrahydrofolate
- Coenzyme B
- Biotin
What You Need To Know About Coenzymes
- A coenzyme is an organic non-protein compound that binds with an enzyme to catalyze a reaction. A coenzyme cannot function alone, but can be reused several times when paired with an enzyme.
- Coenzymes are small molecules.
- Coenzymes are non-protein in nature. They are just organic molecules.
- Coenzymes bind to the active site of the enzyme, activating it.
- Coenzymes alter their structure during the reaction by binding to functional groups released from the reaction.
- Coenzymes are less specific.
- Examples of coenzymes include NAD, ATP, Coenzyme A and FAD.
Also Read: Difference Between Cofactor And Coenzyme
Difference between Enzymes And Coenzymes In Tabular Form
BASIS OF COMPARISON | ENZYMES | COENZYMES |
Description | An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. | Coenzyme is an organic non-protein compound that binds with an enzyme to catalyze a reaction. |
Size | Enzymes are large molecules. | Coenzymes are small molecules. |
Nature | Enzymes are mainly globular proteins. | Coenzymes are non-protein in nature. |
Function | Enzymes act as biological catalysts. | Coenzymes bind to the active site of the enzyme, activating it. |
Change Of Structure | Enzymes’ structure remains unaltered throughout the reaction. | Coenzymes alter their structure during the reaction by binding to functional groups released from the reaction. |
Specificity | Enzymes are very specific to the reaction they catalyze. | Coenzymes are less specific. |
Examples | Amylase, protease, kinase, maltase, fructase etc. | NAD, ATP, Coenzyme A and FAD. |
Comments are closed.