all right Niners in this video we're going to talk about amino acid metabolism so specifically when we talk about amino acids we're going to have to look at each you know a couple different amino acids how they're actually being metabolized and utilized for energy okay so we're going to kind of take what's happening here we're going to take some amino acids that are going to be in the muscle we're going to undergo a transamination process and then we're going to see how what's going to happen afterwards in the liver okay so first thing you know
there's going to be a lot of different amino acids that can be found within our actual muscle here because you know you need amino acids for protein synthesis right so let's say that I have certain types of amino acids in this area let's say I take for a specific one for example let's say I take alanine so I'm going to draw the basic structure of alanine so you can remember an amino acid always has what's called a n c c on this end it's going to have a NH3 group with a plus charge and then
it's going to have a alpha hydrogen and then for this case for alanine it has a methyl group okay so then it has that methyl group now another thing about the alanine is it has a carboxin has a carboxin now this is going to be the zwitter iion form of alanine zwitter iion meaning it has a plus and negative charge but the overall charge is neutral this right here is going to be alanine you know what I can do with this alanine I can utilize it for energy when it's the body I'm going to take
this alanine and I'm going to react with another molecule I'm going to react with a very specific molecule and that molecule is going to be called Alpha ketoglutarate so you know Alpha glut8 is going to have something like this so you're actually going to for example you know it's actually derived from uh specifically glutamat so let's say I have an NH3 group here for a second then I have this carbon here with the hydrogen then I have the carboxy group and then usually it actually is coming from glutamate which is ch2 ch2 and then it
has a carboxy group over here okay but instead of having this amine group Alpha ketoglutarate just has a double bond here so you're going to have a double bond right there and this is going to be specifically our Alpha ketoglutarate this is our Alpha ketoglutarate right here so who is this molecule this is specifically Alpha Keto glutarate I'm going to just denote it a k g Alpha ketoglutarate what happens is I'm going to have a specific enzyme and what this enzyme is going to do is it's going to take this alanine and it's going to
take these Al this Alpha ketoglutarate and it's going to react with both of them so let's say that I take for example here I take alanine and I take Alpha ketoglutarate and what I'm going to do is I'm going to react these puppies in a special enzyme so for example I'm going to take here let's say here is my enzyme okay on one pocket I'm going to have the alpha ketoglutarate so for right now I'm just going to show Alpha ketoglutarate here okay in the other pocket I'm going to have over here alanine you know
what I'm going to have right here in the middle let's fix our alanine there guys that should be a l a n i e right then if what I'm going to do is right here in the middle I'm going to have a special molecule this special molecule is going to be called parox phosphate you know paradoxal phosphate is actually a derivative from vitamin B6 you know what happens here what's special about this alanine this alanine has a amine group that's what makes him really really special and this Alpha ketoglutarate has this specialized oxygen what happens
is this paradoxal phosphate is going to act as the transferring structure because you know this parod oxal phosphate is actually linked with this enzyme through what's called a sh shift based linkage shift Bas linkage now remember it's not what you think it is it's called shift base okay so this enzyme right here is linked to that perod oxal phosphate through a shift base linkage you know what that is uh just by structure you never heard what's called an an emine this is from organic chemistry an emine an emine is just basically when you have a
carbon here double bonded to a nitrogen like this who could be bound to maybe like should say a methyl for that case and who's going to have some type of General structure like this this is an emine that is how this enzyme is linked to the paradoxal phosphate through a shift based linkage now what this enzyme does is it takes the amine group from the allany and gives it to the paradoxal phosphate then this paradoxal phosphate takes that amine and gives it to the alpha ketoglutarate then another thing that happens this Alpha ketoglutarate gives his
oxygen onto the parod oxal phosphate and the paradoxal phos phate gives this oxygen onto the alanine so in other words these two molecules are just swapping what let me Circle What specifically is being swapped this is being swapped and this is being swapped and as a result look what happens as a result of these two molecules reacting here so I'm going to take this guy here and I'm going to take this guy here and you're going to get two new molecules now question is what is the name of this enzyme that's actually causing this process
to occur we're going to abbreviate it called alanine so Al Amino trans trans aminase so alanine Amino trans aminase so this is a transaminase enzyme so again what is this enzyme here called specifically he's called alanine Amino transferase or transaminase so we're going to stick with trans aminase okay what is this enzyme going to do he's going to take the amine group from the alanine give it to the paradoxal phosphate who gives it to the alpha ketoglutarate the alpha ketoglutarate is going to give the paradoxal phosphate its oxygen which is going to give it to
the alany as a result these two guys are going to swap now look what happens to the alany now this alany is now going to have a double bond oxygen right there so now you're going to have a carbon double bond oxygen with the methyl group and then what carbon double bond oxygen if you guys know a little bit about your structures here from biochemistry this right here is pyruvate how many carbons is it one two three I know we've show it showed it simply which just circles but this is specifically pyruvate that is pyruvate
now I have this pyruvate here that I under had underwent this process called called transamination all this transamination process is is that this alanine is doing what he's giving his amine group to Alpha ketoglutarate then what this Alpha ketoglutarate is doing what he's giving his oxygen to the alamine and this Alpha ketoglutarate is becoming a new molecule so now wherever this oxygen is put an amine group and what are you going to get out of this process so now we're going to get rid of that actual oxygen group and we're just going to replace it
with a amine group then we're going to have over here we're going to have the carboxy end so just the co negative here I'll put the double bond for those of you who want to see it I'm put the double bond oxygen with the O negative charge and then coming down what am I going to have I'm going to specifically have a hydrogen right here and then a ch2 ch2 and then a carboxy Groove you know what this molecule is called this molecule is called glutamate this molecule is called glutamate okay so what happened within
this process and what is this process here called let's define what this process is called This is called trans amination all trans amination is is I am taking the amine group from an amino acid in this case it just so happened to be alanine it could be many many different types of amino acids so I can take this am group from the alanine and I'm going to transfer it to who to this keto acid what is this keto acid called Alpha ketoglutarate so this is called a keto acid keto acid you might recognize him as
a kreb cycle intermediate so he's a kreb cycle intermediate then this Alpha ketoglutarate is giving his oxygen to the alanine and then this alanine will turn into pyruvate and then when the alpha ketoglutarate gains that Aman group he will turn into glutamate now this process is catalyzed by a alanine aminot transferase enzyme which is having a shift based linkage with the paradoxal phosphate all a shift based linkage is is it's just going to be an emine and an amine is just the carbon double bounded to a nitrogen right in this form then this paradoxal phosphate
is playing a very important role in being able to transfer the amine to one guy and then the oxygen to the other guy now we what can we do with this pyruvate and what can we do with this glutamate that's the question now in the muscle cell you know what you can do with pyruvate what can I do with the pyruvate in the muscle cell you know I can take this pyruvate and I can do two things with him one thing is I can convert him into lactic acid okay and then the other component is
I can take and convert him into acetal COA where can acetyl coo it can go into the you already know this guys the kreb cycle and then from the kreb cycle you can go to the electron transport chain and then the electron transport chain will allow for the production of ATP so look what I just did there with this whole transamination process I did I did two things one is I turned alanine into pyruvate that pyruvate can then do what it can get converted into lactic acid or it can get converted into acety COA the
acetylcoa pathway will ultimately lead to the production of ATP energy production what will happen with this lactic acid watch this you guys remember this this is called the Corey cycle what happens with the lactic acid you know the lactic acid is going to do what it's going to come into the blood and we're going to we're going to zip through this guys so what happens with the lactic acid the lactic acid is going to be what it's going to be converted into pyruvate in the liver you know by specifically by the lactate dehydrogenase enzyme it's
stimulating this step and it's taking NAD D what NAD positive and converting it into NAD H then we're taking that pyruvate and we're doing what we're converting it eventually into glucose six phosphate and then only in the liver do they have that specialized enzyme let's put that enzyme here in red this enzyme is called glucose 6 phosphatase and this enzyme is stimulating this step and then what are you going to get as a result here you can get free glucose and that can get taken back into the muscle right through the Corey cycle what is
the whole purpose of this I helped with this process of gluconeogenesis so what are the two Fates then so far of this actual transamination process one is that can lead to the formation pyruvate and that pyruvate can either go and make ATP energy formation the second thing is I can make lactic acid and that lactic acid can do what it can get taken up by the liver and get converted into glucose with this glucose 6 phosphatase enzyme being present and this is called glucon neogenesis okay what about this glutamate what's so special about him what
can happen with this glutamate let's come over here and let's bring this glutamate over to the liver because that's what he's going to do he's going to come from the muscles or even other different tissues cells and come to the liver okay so now we're going to have this glutamate that we brought over from the muscle so this glutamate it has that Amin group right there right that amine group is going to be very very special because we're going to want to get rid of it okay so now how does this happen okay there's a
special special pathway here and we have to be very very uh particular about this pathway let's make this a blue line here okay what happens here is there's going to be a special enzyme involved in this pathway and what's going to happen here is I'm going to take NAD P positive okay you guys have probably not seen this one yet this is a very very whenever it forms this next molecule because what will'll happen is it'll come into this reaction and generate nadph this molecule nadph is a very strong reducing agent we use this in
a lot of fatty acid synthesis Pathways and for free radical reactions that we'll talk about okay what I'm going to do is I'm going to take this molecule here who is this molecule again this is our glutamate which is coming from the muscles and it can be coming from other tissues I just picked the muscles as a specific example but many many many tissues do this transamination process that we talked about but now glutamate which is coming from the muscles it's going to get acted on by a specific enzyme in this area that's going to
have nadp positive get converted into nadph which is a reducing agent for fatty acid synthesis and and specific free radical reactions the enzyme catalyzing this pathway is called glutamate dehydrogenase this enzyme is super important because glutamate dehydrogen is going to do two things one is it's going to get rid of this amine group so you see this amine group right here we're going to chop that sucker off and we're gonna release that amine group off of this so you know what else we're going to lose as a result of this let's bring this Arrow up
a little bit more and look what's going to happen as a result two things are going to happen Okay I'm going to release out of this this what ammonia molecule oh man ammonia is extremely extremely toxic extremely toxic we'll talk about why but then what happens is this glutamate dehydrogenase enzyme is going to help to bring nadp positive to nadph and then convert this it goes through another mechanism it actually goes through another mechanism but we're going to go straight to it because it actually has to get hydrated for a second step this is a
two-step mechanism but we're just going to go straight to the end step where we remove the am group off and we add water so we're going to add water into this reaction when we add water into this reaction you're going to get a special molecule look what you're going to get you guys are going to love this look you get your carbon double bond oxygen ch2 ch2 and then the carboxy group right there then I'm going to get another carboxy group right over here this molecule is called you already know what this one is that's
Alpha ketoglutarate so this molecule right here is specifically called Alpha keto glutarate okay now we will talk about this ammonia in another individual video because what's going to happen is this Ammon is extremely extremely extremely toxic so this ammonia you know he's actually going to react with a proton and when he reacts with the proton he forms ammonium and then ammonium is actually going to go into our mitochondria we'll undergo the Ura cycle and we'll talk about that in individual video but we can do something else you see this Alpha ketoglutarate that we actually made
from this converting glutamate into Alpha ketoglutarate with the presence of glutamate dehydrogenase and N positive to NPH this reaction here this whole process that we just discussed this whole process is called oxidative deamination okay this is called oxidative deamination oxidative deamination is where you're taking glutamate and specifically this is occurring mainly in the liver and the reason why is because you're generating ammonia and you want ammonia to be taken into specifically into the mitochondria but this can oxidative damage can occur in other tissues like the muscles just not as significantly but oxidated deamination is where
you're taking glutamate removing the amine group and releasing it out as ammonia and ammonia is extremely toxic it'll combine with this is ammonia and which is extremely toxic it'll combine with the proton to make ammonium and then ammonium can actually be taken into the mitochondria and eventually convert into Ura this glutamate dehydrogenase and this nadp positive to n pH which is a reducing agent whenever it's ripping that am Groove off it's regenerating Alpha ketoglutarate now you know there's other different types of amino acids that can undergo this transamination process so now you know what I'm
going to do with this Alpha ketoglutarate I'm going to react him with a special amino acid so let's say I take and I draw a sparate so you know sparate is going to have it's very similar to glutamate you have the amine group here again and then remember carboxy group but then it's just in instead of two ch2s it goes straight ch2 to carboxin this right here is a sparate all right or aspartic acid right but in this case since he's in the B the base form this is aspartate if he had the hydrogen there
he'd be as spartic acid but specifically we're going to call this aspartate or sometimes they call it you know if I'm pronouncing it wrong they be call aspartate but now what I'm going to do is I'm going to take the aspartate I'm going to react it with the alphaet glutarate so now let me draw this alphaet glutarate from this reaction that we generated up here so now I'm going to have this carbon double bond oxygen specifically with a carox group then I'm going to have ch2 ch2 and another carboxy group and this molecule was specifically
called Alpha ketoglutarate now what I'm going to do is I'm going to do the same reaction that you guys saw before so what I'm going to do is is I'm going to take these two guys aspartate and Alpha toluate and I'm going to react them with each other and if you guys remember there's an enzyme that's catalyzing this process we're not going to go back into the mechanism because you guys should already know it but this enzyme is actually going to be specifically dealing with aspartate and specifically transferring the amine group from the aspartate to
the alpha ketoglutarate and transferring the oxygen from alpha lutate onto aspartate so this enzyme is called aspartate Amino transferase a and again what is the name of this enzyme called it's called aspartate Amino and then specifically you can call it trans aminase but I believe it is interchangeable with transas because what it's doing is it's doing what what's in here in the center which connected through that shift based linkage the perod oxal phosphate and then what would you have over here you could have a sparate I'm going to put ASP and then over here I
can have Alpha ketoglutarate I'm going to put AKG and if I have this Alpha ketoglutarate over here what's special about the aspartate the aspartate if you guys remember has the amine group coming off of it so it has this amine group and then this alphaet glate has that oxygen what happens they're swapping so this transaminase enzyme is taking the aming from the aspartate giving it to paradoxal phosphate who gives it to Alpha ketoglutarate then the alpha kogate is giving the oxygen to perod oxal phosphate who's giving it to aspartate aspartate will gain the oxygen and
look what happens as a result so get rid of this amine group and that hydrogen and then look what happens double bond oxygen carboxy group ch2 Co negative and then look what I get out of this I put an amine group there you guys already know this molecule look at this guy I put a NH3 positive group a hydrogen my carboxy group ch2 ch2 carboxy group what is this molecule that I formed here this molecule is called glutamate we already talked about him this is glutamate what is this one called this one is called oxaloacetate
okay where can oxaloacetate go if you guys remember let me move this mitochondria out of the way so that we can look at this because you guys will know we'll talk about urea CLE specifically afterwards if you guys remember really really quickly you have aetl COA then you have oxaloacetate which combines with acetyl COA to make citrate citrate gets converted into isocitrate isocitrate gets converted into Alpha deuterate then into suxin COA then into soate then into fumate and then into malate and then into oxaloacetate if you guys remember we took what we took the pyruvate
right we have pyruvate coming into this guy who funneled into pyruvate who do we actually undergo this transamination process to make pyruvate we had alanine all n he can get converted into pyruvate through this transamination process then oh a sparate I could take a sparate and I could undergo transamination process to to make him oh what about glutamate you know glutamate can do the same process also what can glutamate form if he undergoes transamination processes because you know this reaction here where you take glutamate and oxaloacetate being formed from aspartate and Alpha deuterate really this
is reversible and the same way this is reversible what do you think over here is going to be over here is also reversible so not only can I take alanine and Alpha ketoglutarate to make pyruvate and glutamate but I can take glutamate and pyruvate to make alanine and Alpha ketoglutarate that is so beautiful that this enzyme is reversible and it can allow for this process as well as this enzyme so that means what that means that glutamate can react with oxaloacetate to make aspartate and Alpha glutarate so that means glutamate can feed into this one
here what this is showing you is is something very very interesting that I can take a sparate and convert into OA I can take alanine converted into pyruvate I can take glutamate and converted into Alpha hutter you know there's many many many amino acids that you can use in different steps so many different amino acids but you know these aren't the only amino acids that can be involved in this process there's so many other amino acids we're not going to go over every single one of them but to give you an example you know fate
I can actually utilize a specific amino acid called tyrosine and I could take tyrosine I can convert him into fate through different types of mechanisms I could make suino COA I could do this through specific types of mechanism utilizing veine so I could take veine and convert that into suino and I could even have certain amino acids made into aceto COA you know specifically maybe I could take for example even uh Lucine you know so maybe Lucine I could turn turn into aceto there's many many amino acids that can be converted into many points within
this actual either this transition step or CB cycle why is that significant because two things can result out of this what are the two sign ific things that can result if it goes and gets utilized in the KB cycle can't that make ATP yes that can that's one significant component what's the other significant component remember how from gluconeogenesis some of these actual molecules can get converted into OA and then what can happen to the OAA you guys remember that the OA gets converted into malate and then what happens to that malate it gets pumped out
through the malet to sparate shuttle right that malate then gets converted back into oxyacetate and oxyacetate if it's acted on by Pepsi K what can happen it can get converted into phospho enol pyu because this step is irreversible this step right here but this step is reversible and then I can take pep up eventually to glucose so Pepsi K is stimulating this step so in other words what is the significance of this amino acid metabolism I can use amino acids to make ATP or or I can use amino acids to make glucose what is that
call whenever you make glucose from non-carbohydrate sources like amino acids they call it glucon neogenesis wow that's beautiful okay and then again what is significant about these transamination processes that if you have the transamination process and you form a lots of glutamate because that's usually some of the Bas the main products of transamination if you noticed what do we get from this transamination reaction glutamate what do we get from this transamination reaction glutamate you're going to get a lot of glutamate produced in these processes and then what can happen is that glutamate can actually be
acted on by glutamate dehydrogenase that glutamate dehydrogenase will then be taking NP positive to make NPH which is a reducing agent for fatty acid synthesis and free radical reactions and it's going to add water in the second step to make alpha heog glutarate but it's going to remove out of it ammonia and then what can happen to ammonia he can go into the mitochondrial he'll go through the Ura cycle to convert the ammonia into a less toxic form called Ura which we'll talk about in another video last thing guys since you can find these enzymes
in many different tissues you can find this uh specifically this sparate Amino transferase and you can find this Amino alanine Amino transferase you can find this in the heart you can find this within the skeletal muscles you can find it within the liver why is that important because you know let's say for example this liver is damaged tissues are damaged you know what it can release out into the blood if it's actually damaged it can release out this a enzyme you know if this actual muscle skeletal muscle or cardiac muscle is damaged you know what
can release out into the blood alt enzymes why is that significant because let's say that you run a blood test you think that there maybe there's some type of suspection of uh maybe a myocardial farction or liver damage you find out that their blood test comes back and they have elevated a enzymes and elevated ALT enzymes this is indicative of someone having possible liver damage Dage or maybe even primarily cardiac tissue heart damage okay so if you find elevated a alt and maybe even some elevated creatine cyas levels and troponin you might even assume oh
man this person might have had a heart attack or if they have elevated as enzyme levels they might have possibly some type of liver damage all right guys I hope all this made sense I really hope you guys enjoyed it if you guys did hit that like button comment down the comment section and please subscribe in the next video guys we're going to hit the Ura cycle until next time
