Recap: Glycolysis

What happens to Pyruvate?

Howdy my biochemians,

This week as i learnt about the FATES OF PRYRUVATE……

After glycolysis has ended the 2 molecules of pryruvate that was formed are now going to be used all for the regeneration of NADH.

The following is a summarised table of what happens next……


There are three ways the NADH can be reformed and under two conditions either anerobic or aerobic.

First in the aerobic condition…

1) Pyruvate can be converted to acetyl-coA to enter in the Krebs cycle


Under anerobic conditions

There is the conversion to lactate


and there is the fermentation process


Those are the ways in which the NADH is regenerated to be used again in the glycolysis pathway again.

So we are in Week 10 that means only 3 more weeks for the semester to over….


Everyone is excited for the SUMMER VACATION….like me!

Just remember as we approach finals…. ūüė¶

Don’t give up remember

Till I post again…..


Shanice ūüôā

Enzyme Catalyzed Reactions In GLYCOLYSIS

Hi ,it’s me again ūüôā


This is my wordle on the enzymes used in glycolysis.


The order of these enzymes in the glycolysis reaction are:

The first five enzymes are found in the preporatory phase

1) Hexokinase



2) Phosphohexose isomerase



3) Phosphofructokinase-1



4) Aldolase



5) Triose phosphate isomerase


The next five enzymes are found in the payoff phase

6) Glyceraldehyde 3 phosphate dehydrogenase



7) Phosphoglycerate kinase



8) Phosphoglycerate mutase




9) Enolase



10) Pyruvate Kinase


Till next post….



Enzymes Podcast Review

Howdy to all bloggers, am here again with a review of an Enzyme podcast I watched.

In addition to what was mentioned in my first post on Enzymes, this podcast explained how enzymes are turned on and turned off.

Using the lock and key hypothesis for explaination the video used the reaction of hydrogen perioxide which forms the products water and oxygen and the enzyme used was catalase.

Some points that were mentioned in this podcast are:

1) Enzymes are turned on by the presence of cofactors which are inorganic eg.heme which has iron structure present and is used to transport blood (haemoglobin)

They are turned on as well via coenzymes which are organics which helps enzymes work and the example used was thiamine (B1)

2) The video also stated how enzymes are turned off via competitve inhibition as well as allosteric inhibition.

Competive inhibition-when an inhibitor   binds to the active site the reaction does not occur becaus eof the the competing of the inhibitor with the substrate for the active site.

Allosteric inhibition- this is changing the shape type of inhibiton where the inhibitor binds to the allosteric site changes the shape of the active site.

3)It also stated that the rate of the reaction is used to measure the amount of products formed or the amount of reactants that are being used.

At the end of this podcast, my opinion of it was that it lacked alot of information like the different type of inhibitions as well as explain the whole lock and key hypothesis as well as to describe the induced fit hypothesis. Besides this I thought the use of the example was a great way of explain how the the products are formed as well as the used of animation and pictures.

Below is the link to the podcast which is not very long….

See you soon…

NO TIME…………….

So for the past few weeks I was bombarded by a lot of my peers at school asking me “how do i get time to write on my blog?” ¬†“How long do you take to write one.” So i decided I would answer their ¬†questions here as well as leave any tips on how to keep up with your blog entries.

Right now I know some of you feel like this >


I wouldn’t say I have the best solution, but I would just share with you how I keep up with mine…..

I know as the semester is progressing and the workload is getting harder,assignments due, labs and other course work due, we need to realize though that this a course work assignment that is worth 10% and the same energy we put into completing other assignment is the same we need for this blog…… I know this was a completely different idea of an assignment due to problems some students have like expressing themselves even those who might not be that versed in computer literacy but we need to try!!!!

I really just have two ideas of how to keep up with your blog…..

1) Designate two days in the week and stipulate a time frame which can be devoted to your blog……(this helps me a lot)

2) JUST HAVE FUN WITH IT………..( Once you start typing you may not want to stop)

Some of you maybe saying REALLY?!?!?!?………… this is just how i keep up so am just sharing it with you

So as we continue on this challenge I just encourage you to keep going its just like an ordinary assignment, at the end of the day you would want to achieve the best result so DON”T GIVE UP!!!!!!!


From a caring and concerned colleague to you

God Bless……..

Recap: Enzymes

MCQ’s on Proteins and Enzymes

Hey guys,welcome back!!!

Just reviewing the topic on Amino Acids and Proteins,the following are some multiple choice questions for you to try out!! Hope u enjoy

1. What reaction does two cysteine molecules use to form cystine

A. oxidation

B. hydrolysis

C. reduction


E. None of the above

2.  Which of the following is the class that enzyme with EC number

A. ligases

B. transferases

C. oxidoreducatases

D. hydrolyases

E. All of the above

3.    Enzymes are found under which type of protein:

A. fibrous

B. membranous

C. fibrous and globular

D. globular

E. All of the above

4.    How many amino acids is needed per turn of the alpha helix?

A. 3.25

B. 6.3


D. 3.06

E. 3.78

Select the correct multiple answer using ONE of the keys A, B, C, D or E as follows:

A. 1,3,4 are correct

B. only 3 is correct

C. 2 and 4 are correct

D. 1 and 3 are correct

E. all are correct

5. Which of the following bonding in proteins is/are considered not common but is the strongest?

1. hydrophobic interaction

2. hydrogen bonding

3. disulphide bridge

4. ionic bonding

To answer, please leave a comment below…..



The topic Enzymes is quite a familiar one to us as we were all taught this at some time in out high school years.

Now we would look into it a little further….

So a recap…..

What is an Enzyme?


Well i hope u guessed write and said that they are biological catalysts that speeds up a chemical reaction by providing an alternative pathway with a lower activation energy.


What are they made up of?

So hopefully you looked at my previous posts and saw that they fell under the topic of protiens,that is of tertiary structure.

So here are some common terms and definitions that are associated with enzymes.

The transition state of an chemical reaction is the highest arrangement of atoms that is intermediate in structure between the structure of the reactants and the structure of the products.

The activation energy is the minimum amount of energy that is required for the reaction to occur

The number of molecules of substrate converted to product per enzyme molecule per second is called the turnover number or kcat.

There are 6 major classes of enzymes.

1. Oxidoreductases

2. Transferases


4. Lysases

5. Isomerases

6. Ligases

The E.C (Enzyme Commission number) tells you what is the name of the specific enzyme. The first number of the E.C number is tells us the class in which the enzyme belongs to.

e.g. E.C. is called glucokinase as is a member of the class transferases. Note the importance of the order of the classes of enzymes as the number is what corresponds to a specific enzyme.

The following link is animated video showing how enzymes work. Hope you enjoy it just gives a little understanding of the formation of an enzyme-substrate complex!

Sneak Peak into ENZYMES

Keep these key words in mind as I begin to explore the topic enzymes in subsequent posts.....

A little joke:


Recap :Amino Acids



Learning about the world of biochem, in a fun innovative way :)

Joel Osteen Ministries

Joel Osteen Ministries

A little biochem never hurt nobody :)

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Those who are interested in biochemistry (and its relations) are welcomed to indulge themselves in whatever wealth of information this blog has to offer as well as become fully interactive with those who wish to share their views on various topics by so helping each other learn whilst also feeding off what i have to offer as a biochemistry student


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