Class Notes (834,991)
Canada (508,850)
Biochemistry (847)
Prof (22)
Lecture

Biochemistry Lecture No. 15.docx

2 Pages
94 Views
Unlock Document

Department
Biochemistry
Course
Biochemistry 3380G
Professor
Prof
Semester
Fall

Description
Biochemistry Lecture No. 15: Metabolism & Enzyme Regulation th Thursday October 11 , 2012 Metabolism -Metabolism is the sum of all reactions that go in the cell (half of them being catabolic, half anabolic). Metabolic Pathways: -Metabolic pathways are a series of reactions coupled together that form a new product. Flux is the rate of conversion from the reactants to the final product of a metabolic pathway. This conversion is efficient when the net ΔG for the whole pathway is negative. Generally, a metabolic pathway consists of mostly reactions at equilibrium (ΔG ≈ 0), but some are reactions with great spontaneity (ΔG << 0) and are considered crucial. -With equilibrium reactions, where ΔG ≈ 0, changes in concentration heavily influence the extent of the reaction by way of le Chatelier’s Principle. Enzymes used here can catalyze both the forward and reverse reactions and are considered reversible. With highly spontaneous reactions, where ΔG << 0, adding products has little to no effect on the equilibrium of the reaction (which is hardly observed). There is practically no reverse reaction observable as the E Aor the reverse reaction is much harder to overcome. -As irreversible reactions drive the overall process of metabolic pathways, the cell must increase the activity of the enzyme(s) catalyzing only those “steep” (energetically favourable) reactions. Thus, irreversible reactions are the target of regulation. Methods For Controlling The Rate Of Reaction: -Rates of reaction in metabolic pathways can be manipulated in several ways: by changing the amount of the enzyme expressed (during transcription, translation, or degradation), changing the concentration of the substrate or product (using le Chatelier’s Principle), or by changing enzyme activity (through allosteric regulation, covalent modification, or association with a regulatory protein). Changing enzyme abundance often takes very long to take effect and changing substrate or product concentration is often impractical for the cell, while changing enzyme activity usually produces the quickest results. Allosteric Enzymes: -In allosteric enzymes, the shape of the active site (where the substrates binds) is changed by the binding of an effector at a different site known as the allosteric site. Allosteric enzymes are usually multimeric and contain more than subunit. Multimeric Allosteric Enzymes: - Allosteric enzymes are usually multimeric and contain more than subunit. There is a distinction between these subunits as regulatory subunits have binding sites that activate or inhibit its protein’s activity (through the allosteric site), while catalytic subunits help the proteins catalyze a ch
More Less

Related notes for Biochemistry 3380G

Log In


OR

Join OneClass

Access over 10 million pages of study
documents for 1.3 million courses.

Sign up

Join to view


OR

By registering, I agree to the Terms and Privacy Policies
Already have an account?
Just a few more details

So we can recommend you notes for your school.

Reset Password

Please enter below the email address you registered with and we will send you a link to reset your password.

Add your courses

Get notes from the top students in your class.


Submit