Hey guys,
So the project for Biochemistry this semester was a video project. My group decided to based our video on Beta oxidation, giving the necessary steps and explaining them in detail. Please give us your support by looking at the video and commenting if you so desire.
Many Thanks.
Brandon.
This quiz is purely on enzymes only.
1. What class of enzymes breaks down substrates by adding or losing, hydrogen and oxygen?
A) Hydrolases
B) Transferases
C) Oxidoreductases
D)Ligases
2. Ligases is the only one of the six major classes of enzymes to
A) Undergo hydrolysis
B) Combine molecules
C) Oxidise a substrate
D)Rearrange the structure of a substrate.
3.Uncompetitive Inhibitors binds to
A) Active site only
B) Enzyme-substrate complex only
C) Both the free enzyme and enzyme-substrate complex
D) To the substrate molecule only
4. Mixed Inhibitors binds to either the free enzyme or to the enzyme-substrate complex. How does this affect Vmax and Km?
A) Nothing is affected
B) Vmax increases and Km can increase and decrease
C) Vmax is reduced and Km can increase and decrease
D) Vmax remains constant, while Km increases
5) Which type inhibitor binds only to the active site?
A) Non-competitive
B) Uncompetitive
C) Competitive
D)Mixed
Best of luck.
Thank you for you time.
What is an Inhibitor?
An inhibitor is any substance that diminishes the velocity of an enzyme catalysed reaction.
There are two main categories of inhibition- Reversible and Non-reversible. This entry deals with reversible inhibitors only. There are four types of reversible enzymes.
These are:
Competitive inhibitors.
These inhibitors compete with the substrate molecules for the active site of the enzyme. Competitive inhibitors only bind to the active site of the free enzyme, note that it never binds to the enzyme-substrate complex. Competitive inhibitors do not change the Vmax, maximum velocity, of the reaction, however the substrate affinity binding to the active site of the enzyme, decreases. This means Km increases. (Remember high affinity = low Km and vice versa) .
Taken from http://www.MyMcat.com
In the case of allosteric enzymes. Both substrate and inhibitor cannot bind to the enzyme at the same time. When the Inhibitor binds to one active site, it temporarily changes the shape of the other active site, preventing the substrate from binding.
Taken from “Describe an Induced fit model” , http://www.tokresource.org
Non-Competitive Inhibitors.
Unlike competitive inhibitors,which only bind to the active site of the enzyme, non-competitive inhibitors can bind to the free enzyme as well as the enzyme substrate complex. Since the substrate can still bind to the enzyme, this tells us that Km is unchanged, however Vmax is reduced as the enzyme does not function with the inhibitor.
Taken from http://www.mymcat.com/wiki/Enzyme_Inhibition
Uncompetitive Inhibitors.
These inhibitors only bind to the enzyme substrate complex. This means that the substrate can bind to enzyme although the inhibitor is already bound to it. This also tells us that both Vmax and Km are reduced.
Taken from http://www.mymcat.com/wiki/Enzyme_Inhibition
Mixed Inhibitors.
Mixed inhibitors get the term “mixed” because they can act as competitive inhibitors, and only bind to the active site, or act and uncompetitive inhibitors and bind to the enzyme substrate complex. As a result of this, substrate affinity to the enzyme can either increase or decrease,(i.e. low or high Km values). From uncompetitive inhibitors, Vmax will always be reduced as the presence of the inhibitor decreases the velocity.
The lock and Key hypothesis was brought about Emil Fisher in 1894. According to the video, enzymes are specifically shaped to match their preferred substrate. This hypothesis greatly shows the specificity of enzymes, however it does not explain the transition state that enzymes achieve.
Most substrates do not fit perfectly in the active site of enzymes. Daniel Koshland, 1958, proposed a new model, called the induced fit model. Enzymes being globular, flexible proteins, reshape their active site to better support the substrate they bind to. Bear in mind that, reshaping to fit the shape of the substrate does not permanently change the structure of the enzyme. The enzyme remains unchanged and ready to bind to more substrate.
There are six classes of enzymes and they should be learnt in this specific order:
This is the order in which we assign an enzyme commission number (EC), which is a numerical number, based on the reactions they catalyse. For example, Adenosinekinase (E.C.2.7.1.20) is used to transfer a phosphate group from ATP. The two in the E.C number means that it belongs to the group transferases.
Oxidoreductases.
These enzymes catalyses all redox reactions in which oxygen or hydrogen are gained or lost. Examples of these are peroxides, lactate dehydrogenase.
Transferases.
These enzymes are responsible for the transportation of functional groups of molecules such as amino groups, acetyl groups or phosphate groups. Examples of these are alanine kinase. (Kinase’s transfers phosphate groups)
Hydrolases.
These enzymes , affect substrates via hydrolysis. (i.e Adding water.) Eg. Lipase or sucrase.
Lyases break down molecules by removing groups of atoms without going throught the process of hydrolysis. For example, Oxalate dehydrogenase.
Isomerases.
Enzymes of this class re-arrange the atoms of the substrate they bind to. Example, Glucose phosphate isomerase.
Ligases.
These enzymes combine two molecules together using energy received through the break down of ATP to ADP. Most common example, DNA ligase.
biochemanics 