Hey guys ! It’s me again 🙂 giving yet another posts on enzymes. Whooo hooo!!
Okay so before we get started I thought i’d make reference to the very informative videos that I have obtained all my information which I am about to summarize for you 🙂
Video Link :
So let’s start shall we!
Summarizing, as we’ve learnt before, enzymes are biological catalyst which can speed up the rate of a chemical reaction by providing an alternative pathway for the reaction to occur at a lower activation energy.
Let’s pause for a cause here :
What do we mean by activation energy?
Well activation energy refers to the minimum amount of energy for a reaction to occur.
Okay. We can continue 🙂
As seen in the video, some RNA molecules or ribozymes can act as enzymes since they are substrate specific, enhance reaction rates, and emerge from the reaction unchanged.
Again. Let’s pause.
What are some features of these biological catalysts? ( ….. you might ask.)
- They have catalytic power, meaning the ability to speed up a reaction while the molecule itself remains unchanged.
- They can be regulated or controlled in some way
Also something fascinating noted in the video was that some antibodies, which prior to this I thought dealt strictly with the body’s immune system, have catalytic properties. These special antibodies are referred to as abzymes. This got me thinking about how so many different small little things work together to make our magnificent bodies function properly, as these factors work together. Truly remarkable if you ask me!
Next, in the lecture, a Transition State was mentioned. This referred to the highest energy arrangement of atoms that is intermediate in structure between the structure of the reactant and the structure of products.
Noting that :
structure of substrate ————–> structure of product
So now we ask, how do we name these enzymes?
- based on their substrate : like lipase and sucrose
- based on a description of the action/reaction performed : Example pyruvate carboxlase
- And sometimes, well sometimes we just find outta timin’ enzymes, like trypsin pepsin and catalase
Another way to classify enzymes is by the EC number, where there are six main categories that we should know:
- Oxidoreductoses —> Catalyzes oxidation reduction reactions
- Transferases —> Catalyzes transfer of C, N, or P containing groups
- Hydroloses —> Catalyzes cleavage of bonds by addition of water
- Lyases —> Catalyze cleavage of C-C, C-S and certain C-N bonds.
- Isomerases —> Catalyzes racemization of optical or geometrical isomers
- Ligases —> Catalyzes formation of bonds between carbon and O, S, N coupled to hydrolysis of high energy phosphates.
SO. To be honest. memorizing these categories are gonna be quite a challenge for me. But through practice I think, like everything else we should be able to get the hang of it !:) now that we’ve gotten that FUN part ( extreme sarcasm here) out of the way, we can finally move on to Cofactors!
Cofactors refer to a non protein component which allows an enzyme to function properly.
Cofactors can either be inorganic or organic.
Inorganic cofactors can usually refer to metal ions, examples being Zinc 2+, or Mg 2+
Organic factors however, can lead to something known as “co enzymes” which are frequently derived from vitamins where transparent association can lead to “co substrates” where as permanently associated vitamins can lead to what we know as a “prosthetic group.”
Which leaves me to conclude about inorganic catalyst.
These kids never get 100% of the product and cannot be regulated. Examples where inorganic catalysts are used include the haber process, and the contact processes within the industry .
Alright folks! That’s it for this post! I know there’s plenty more to write about here. Hopefully by the next two days i’ll be able to catch up. Also a new quiz will be coming up soon! so make sure you’re on top of your game! 🙂