Publish Paper 1 Review – Regional Aerobic Glycolysis.

S. Neil Vaishnavi, M. E. R. 2010. Regional aerobic glycolysis in the human brain. Accessed 8th April 2014. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955101/

In this paper an experiment using 33 right-handed neurologically normal young adults at rest was used to calculate the regional distribution of aerobic glycolysis using positron emission tomography. Aerobic glycolysis can be defined as the state where glucose metabolism exceeds that used for oxidative phosphorylation despite sufficient oxygen to metabolize glucose to carbon dioxide and water. It was stated that aerobic glycolysis normally increases with increase cellular activity. This experiment was used to further help understand the role of glycolysis in the human brain at rest. Also to determine whether there is variations in glycolysis in the brain and how this in turns affect overall brain energy utilization.
Aerobic glycolysis is traditionally assessed in terms of the molar ratio of oxygen consumption to glucose utilization and a number less than 6 is indicative anerobic glycolysis is present. From the results gathered it was seen that the regions of the brain with high aerobic glycolysis included prefrontal cortex, lateral parietal cortex, posterior cingulate/precuneus, lateral temporal gyrus, gyrus rectus, and caudate nuclei. Whereas low aerobic glycolysis was found in the inferior temporal gyrus and throughout the cerebellum. Thus from the results it can be seen that the levels of aerobic glycolysis are not strictly related to the levels of brain energy metabolism but factors for ongoing aerobic glycolysis in the brain may be: 1) Energy – because the brain needs to suport membrane bound processes which needs ATP it would need to perform aerobic glycolysis to get the required energy. 2) Biosynthesis and 3) redox states.
Therefore from this research it can be seen that not only brain activity affects the level of aerobic glycolysis but there may be many other contributing factors. Thus research in this area should continue as it may help in the prevention/ curing of brain functioning related diseases.

This article is very appealing and everyone interested in biochemistry should take a look at it!!!! 🙂

N-Zymez homie!

What the heck are enzymes?

You don’t know what enzymes are? Really?! Ok that’s fine. An enzyme is simply a biological catalyst. It speeds up a biological reaction with out being used or changed and it is specific, meaning each enzyme only works on a specific substrate. For example lipase hydrolyses lipids and only lipids. (How do enzymes speed up reactions though? ) OMG glad you asked! They just create a different pathway that has lower activation energy than the original pathway.

Most enzymes are proteins, some are RNA molecules known as ribozymes (they satisfy mostly all of the enzymatic criteria eg. they are substrate specific, they speed up the reaction rate, and they remain unchanged after the reaction. Some antibodies have catalytic properties and these are called abzymes.

What’s the big deal about enzymes?

Without enzymes life is literally impossible! Enzymes allow for respiration to occur. Which means, no enzymes à no energy à no life. Thank goodness for enzymes right? Yeah… trust me I know.

According to Ask.com, in the human body approximately 2700 enzymes can be found. These enzymes are separated into three major groups, which are: metabolic enzymes, food enzymes and digestive enzymes. Their location in the body depends on their function. Enzymes can be found in the mouth in saliva, in the stomach and everywhere else in the body. Without enzymes we are nothing!

This is an energy profile diagram.

This diagram shows exactly how enzymes speed up the reaction to produce product.

But what is activation energy? Activation energy is the minimum energy needed for a reactant to react.

How do enzymes get their name?

Um… their parents obviously name them at birth just like everyone else! No, just kidding. Enzymes are either named based on the substrate they react on, the action they perform, they end in ‘ase’ or they just have some random name that has nothing to do with them. Because names were getting out of hand, our homies at The International Union of Biochemistry and Molecular Biology, IUBMB for short, decided to come up with a naming system. They divided the enzymes into 6 classes. In each class is a sub class and in each subclass there is a sub-subclass. Each is numbered and therefore a series of 4 numbers specifies a specific enzyme (this is called the Enzyme Commission [E.C.] number.

The 6 major classes are: 

1. Oxidoreductases – Catalyze oxidation-reduction reactions
2. Transferases – Catalyze the transfer of C,N or P containing groups
3. Hydrolases – Catalyze cleavage of onds by adding water.
4. Lyases – Catalyze clevage of C-C, C-S an some C-N bonds
5. Isomerases – Catalyze isomerizaton of optical or geometric bonds
6. Ligases – Catalyze the formation of bonds between C and O, S, and N couples to hydrolysis of high energy phosphates.

Holoenzyme?? Hol up.. holo what??

Omg chillllll! Its simple! A holoenzyme is just a biochemical compound that is a combination of an enzyme and a coenzyme. And before you go a-wall!  A coenzyme is just a substance that is necessary for an enzyme to function.

Inorganic Catalyst v.s Biological Catalyst

Well incase you didn’t know, biological catalyst are THEE (emphasis on thee) fastest by far when compared to inorganic ones. Biological catalysts are also the most efficient. For example: during the Haber process, which makes ammonia, the temperature needed is 450 degree Celsius, at 1000 atm! What? Amylase breaks down starch to maltose in my mouth and at less than 100 degrees Celsius! And unless you’re a fire-breathing dragon it does the same for you!

So whenever you’re feeling on top of the world, and feel that you can take on a lion, tiger or bear… give enzymes a quick shout out, because with them my good friend… you are without life.

Here’s some pickup lines! Use them wisely.

In that order!

Chao for now!