What is the difference between a cofactor and a substrate

And we even saw that when we talked about hexokinases, when we talked about the phosphorylation of glucose, we said hey, the way that it lowers the activation energy is you have these positive magnesium ions, these positive magnesium ions, that can keep the electrons in the phosphate groups a little bit busy, draw them away, so that this hydroxyl group right over here can bond with this phosphate and not be interfered with these electrons.

Well these magnesium ions right over here, they aren't officially part of the protein. These are what we call cofactors. So you might have a cofactor right over there that latches onto the broader protein to become part of the enzyme, and you actually need that for the reaction to proceed, it plays a crucial role here.

So another drawing in the textbook, you'll see something like this, or even, they'll draw, they'll say okay, in order for this reaction to proceed, yes, you need the substrate, but you also need the cofactor. The cofactor. And once again, it sounds like a fancy word, but all it means is a non-protein part of an enzyme. It's another molecule or ion or atom that is involved in letting the enzyme perform its function that it's not formally a part of an amino acid or part of a side chain or part of the protein, but it's another thing that needs to be there to help catalyze the reaction.

We saw that with hexokinase, you had magnesium ions that the complex picks up. And this is why, when people talk about your vitamins and minerals, a lot of the vitamins and minerals that you need, they actually act as cofactors for enzymes.

And so you could even see it in this drawing over here, at least based on what I read these are the magnesium ions in green right over here, and these are cofactors. These are cofactors. So cofactor, non-protein part of your actual enzyme. Now, we can subdivide cofactors even more. We can divide them into organic cofactors and inorganic cofactors. So if you have cofactors, we've seen an inorganic cofactor, a lot of these ions, you'll see magnesium ions, you'll see sodium ions, you'll see calcium ions, you'll see all sorts of things acting as cofactors, often times to distract electrons, or to keep them busy so that electrons can proceed.

But you can also have organic ones, you can also have organic molecules. Remember, organic molecules, these are just, they'll involve carbon, they have chains of carbons and other things. And cofactors that are organic molecules, we call them coenzymes. And there's a bunch of examples of coenzymes. This right over here is the enzyme lactate dehydrogenase and it has a coenzyme, and this coenzyme you are going to see a lot in your biological careers, NAD, right over here.

Notice, this isn't just an ion, it is an entire molecule. It has carbon in it, that's why we call it organic. And it is not formally protein, it's not part of the amino acids that make up the protein, so that's what makes it a cofactor, and since it's an entire organic molecule, we call this a coenzyme. But like any cofactor, it plays a role in actually allowing the enzyme to do its function, to facilitate a reaction. Our body definitely has several things going on within it.

With so many different systems in our body, it certainly needs not just one type of reaction, chemical or otherwise, to ensure that it functions as it should. Cite APA 7 Franscisco,. Differences Between Cofactor and Coenzyme. Difference Between Similar Terms and Objects. MLA 8 Franscisco,. A prosthetic group is a tightly bound, non-polypeptide unit required for the biological function of some proteins. It may be organic coenzyme or inorganic cofactor but is not composed of amino acids.

So neither coenzymes nor prosthetic groups can be classified under cofactors. Cofactor bonded tightly to enzyme is called prosthetic group.. Cofactor bonded loosely to enzyme is called coenzyme…. Name required. Email required. Please note: comment moderation is enabled and may delay your comment.

There is no need to resubmit your comment. Notify me of followup comments via e-mail. Written by : Celine. User assumes all risk of use, damage, or injury. You agree that we have no liability for any damages. We shall start by defining each term first.

What is a cofactor? Coenzymes refer to the inactive non-protein organic co-substrates without a protein part or apoenzyme that directly participate in the enzyme catalysis.

Cofactors are classified into two types based on the enzymatic activity, namely inorganic and organic cofactors. The inorganic cofactors include metal ions, while organic cofactors include coenzymes and prosthetic groups. Thus, the coenzyme is a subtype of cofactors. Cofactors constitute a broad group of accessory elements, out of which some may associate covalently or non-covalently with an apoenzyme.

Coenzymes are carrier molecules that join transiently or non-covalently with an apoenzyme. The separation of cofactors from an enzyme is sometimes easy or difficult only separates after enzyme denaturation. As the coenzymes are transiently attached to the enzyme complex, they are easily separable. Dialysability is a property of the ions or molecules through which they can diffuse down a semipermeable membrane or separated by dialysis.

Few cofactors are dialysable like coenzymes and metal ions , whereas others are non-dialysable. The function of the cofactor is to fasten the enzymatic reaction. Coenzymes work as substrate shuttles that help in translocating atoms or groups from one place to the other inside a cell. Leave a Comment Cancel Reply Your email address will not be published.

Separation of cofactors can be easy or difficult separates only after enzyme denaturation. Coenzymes are attached transiently to an apoenzyme and can be easily detachable.