Heme Catabolism and Degradation Pathway Biochemistry. Purine metabolism, involving the conversion of nucleosides to nucleotides and thence to DNA and proteins, is a critical step in heme catabolism. Degradation of hemoglobin requires four enzymes: 3-methyladenine demethylase, furfural dehydrogenase, and cytochrome b5 reductase. Heme degradation also involves two pathways: the oxidative pathway and the sulfur-containing pathway.
Heme catabolism and degradation pathway is responsible for breaking down heme, a nutrient found in blood cells. Heme is essential for the body to produce red blood cells, and when it’s not properly processed, it can lead to health problems. The degradation pathway starts with the heme-binding protein hemopexin, which transports heme from the liver to other parts of the body.
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Heme catabolism and degradation pathway are responsible for the degradation of heme molecules. Heme is a molecule that contains iron and is found in many proteins, enzymes, and other biomolecules. The pathway begins with the transfer of an electron from heme to an acceptor molecule. This process creates a free radical which can damage other molecules. The heme catabolism and degradation pathway is important for the proper function of the body’s cells.
Heme Catabolism and Degradation Pathway Biochemistry
Hey guys. Jj here in this lesson I’ll be talking guys about heme catabolism or heme breakdown. Now, in your body, your red blood cells are continually turning over or being degraded in a process called homolysis. Now, your red blood cell is just a non nucleated cell cell that is mainly composed of a protein called hemoglobin. So a red blood cell is just pretty much like a bag of hemoglobin.
Heme Catabolism and Degradation Pathway Biochemistry It doesn’t really have any other organelles. It doesn’t have mitochondria. It doesn’t have a nucleus. It just is composed of hemoglobin. Now, when your red blood cell is broken down, it will release hemoglobin.
Now, hemoglobin is a protein, a protein molecule that contains four polypeptide chains, two Alpha like chains and two beta like chains with a heme prosthetic group. Now, the heme prosthetic group contains an iron mute in the center of it which allows it to bind to oxygen.
Now what will happen is the hemoglobin and the other components of the broken down red blood cell will be taken up by the reticulo endothelial system. Now you may be wondering what is the Reticula endothelial system? Well, the reticulum endothelial system is just your white blood cells, macrophages and other white blood cells.
So your leukocytes. So your white blood cells will come along. They’ll engulf the red blood cell remnants along with hemoglobin. And what they’ll do is hemoglobin will actually be processed into heme and the protein portion of hemoglobin, the polypeptide change will be broken down into free amino acids which can be used later to produce other proteins. Now, the heme group itself is toxic.
Heme degradation Biochemistry
The body needs to get rid of it in some way. So what it’ll do is it’ll actually convert heme by the enzyme heme oxygenase. It’ll convert heme into Billive Verdon by the enzyme heme oxygenase. Now, I’ve got the text here, the boulevardin text in green color. And that’s because Boulevard is actually green in color.
It’s pigmented and it has a greenish color. And so there’s a few things that will be required in this process from heme to billiverdon.
What you’ll need to undergo this process is that you’ll need three oxygen and an NADPH to perform this conversion from heme to billiverdon. And what will also be produced from this reaction is carbon monoxide which will be exhaled. And you will also actually release the iron from the heme group.
So you can see here Bill Verdon actually is missing iron so that iron will actually be stored as ferritin or hemispheterin within the white blood cell. Now once you have Bila Verdon, what will happen is it will undergo another enzymatic reaction by the enzyme biliverden reductase to bilirubin.
Heme catabolism ppt
Now, like biliverton, bilirubin is actually a pigmented chemical and it’s actually Orange in coloration. Now, like the previous reaction, the reaction from billiverdon to billowrubin also requires NADPH. So just remember guys that for these couple of steps you need NADPH. Now, NADPH is produced from the Pentos fossil pathway so just remember that and also an important note is that since these are both pigmented chemicals this is actually the cause of the change in coloration of bruising So when you bruise you’ll have a breakdown of red blood cells you’ll get beliverted and then it’ll be converted slowly into bilirubin so that’s why you see that change in coloration in your tissue from a bruise .
So I thought that was just interesting information now once you have Bilirubin what will happen is the bilirubin is actually lipophilic it’s actually not hydrophilic in nature so it needs to be conjugated So at this point when you’re in the blood, when you have Bilirubin in your bloodstream it has a hard time being transported through the blood because of the blood is an aqueous solution so what it will have to do is Bill Rubin will have to be bound to albumin and again albumin as always is the most abundant protein or most abundant protein in your serum.
so then Bilirubin gets bound to Albin and transport in the blood So once that happens your blood will as always go to your liver now what will happen is the albumin will drop off bilirubin to your liver to a Hepatocyte So your Bilirubin is released into the Hepatocyte it actually binds to a receptor known as ligandin I don’t have it in the scheme but it’s called ligandin then Bilirubin is actually conjugated to UDP glucularide So in
Heme degradation in humans
Heme degradation in humans. actuality it’s actually two UDP gluculars that are conjugated to Bilirubin by an enzyme called UDP glucorenil transferase one and two there’s actually two enzymes that perform this process and then you’ll have a conjugated Bilirubin So Bilirubin glucorinide or a bilirubin with two glucorinate muietes attached to it So once you have that conjugated bilirubin in your hepatitis what will happen is it’ll be released and incorporated into bile within the gallbladder now when bile is released from your gallbladder into your small intestine it .
will also release the bilirubin as well So Bilirubin is then released into your small intestine now since your small intestine is just full of intestinal bacteria or intestinal flora those intestinal bacteria will actually oxidize the bilirubin into something called Uroballinogyn Uroballogen will then also be processed again by other species of intestinal bacteria into strocobillin and circobillin is actually also a pigmented chemical and the strobillin will actually be excreted in your feces now.
circobillin is actually Brown in coloration that’s why your feces are actually Brown in coloration now not all urable energy will actually be converted into circlebillon in the stone intestine some of it will actually be released into or will actually be reabsorbed back into your bloodstream or into a blood vessel and what will happen.
is it’ll be transported in your blood uralanogen be transported in your blood to the kidneys and then what will happen is the uroblanogen will be converted into urobillin which is then excreted in your urine now urobillin again is a pigmented molecule and it’s yellowish in coloration, which is the reason why your urine is yellow.So I thought that was interesting, guys, that this is kind of the main reasons for why you see different discoloration in different areas of your body.
heme degradation slideshare
heme degradation slideshare So just as a summary of heme catabolism, we have red blood cells. And I just want to give you Some quick facts about red blood cells. Each red blood cell has approximately 270,000,000 hemoglobin molecules. So every time your red blood cell Is being broken down by hemolysis, you’re getting a humongous release of hemoglobin that needs to be processed and the heme groups need to be excreted from the body.
A typical red blood cell has a lifespan of 120 days. So as you can imagine, this process is continually going on. You always have different aged red blood cells that are continually being broken down. And because there’s a continuous breakdown of blood cells, there’s actually 100 to 200 million red blood cells are broken down each hour. And red blood cells are typically broken down within the spleen.
Because the spleen has very small vessels which the blood cells go through, they get squeezed through the spleen, and the spleen kind of just tests the strength of red blood cell membrane. And if the red blood cell is old or damaged, It’ll be broken down in the spleen. But red blood cells are also broken down at a smaller degree in the liver as well. Now for hemoglobin hemoglobin, about 6 grams per day of hemoglobin is degraded in the body. Just because you can imagine there’s a lot of hemolobin molecules Being broken down all the time.
Now for bilirubin, there’s about 300 mg per day of bilirubin being produced. And now in adults, the blood serum level of bilirubin is actually typically looked at in a couple of different ways. Conjugated bilirubin typically is in concentrations Ranging from zero to five micro molars per liter or zero to 0.3 milligrams per deciliter. And the total amount of bilarbin in blood serum Is three to 22 micro molar per liter, or 0.2 to 1.3 milligrams per deciliter. Now, neonates are a different story.
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Conclusion
heme catabolism and degradation pathway play an important role in the synthesis of proteins and other cellular molecules. This article has provided a general overview of this process, and readers are urged to explore further resources for more understanding. Readers may also wish to consider how heme catabolism and degradation pathway might be involved in their own health and well-being.
