BIOCHEMISTRY PART II NEET MDS INICET MDS Quick Revision WE ARE WITH YOU

hi everyone this is dr saithi team mds conquer so let's have a quick revision of your biochemistry protein metabolism so if you see these are the elemental composition of proteins where they are where it is constituted by five major elements that is carbon hydrogen oxygen nitrogen and sulfur so the composition is quite important so exactly the numerical value it might be asked so just have a look of this so amino acids are nothing but they're organic compounds which consists of two functional groups that is amino and carboxyl okay so amino group is basic while as carboxyl group is acidic in nature okay so this is regarding the simple introduction so coming to the protein structure so what is primary what is secondary what is circular and what is quaternary okay so secondary is like a helix and chains of polypeptide chains are with tertiary and the complex of the protein molecule is with the quaternary ok so various functions of the protein if you see they are called as a working horses right so why because they have very good functions exhibited so see you can see all the functions that they provide structural components they help in movement of the muscles they store the nutrients they carry the essential substances throughout the body they regulate the body metabolism okay and they catalyze the biochemical reactions as well as recognize and also destroy the foreign bodies okay so these are the important functions next what are the essential and non-essential so this is quite important okay so i think you know it so just give a good glance to this next based on the structure again it is again divided as aliphatic aromatic acidic basic hydroxylic sulphur containing an amidic dick amide or medic and acidity okay so if you see here the names which comes under aliphatic are all these okay so at times if they want to post a memory based question though definitely they can ask from here so even have a look of the classification based on the atomic structure and based on the composition okay and again based on non polar and polar groups negatively and positively charged so this is one more classification so even have a look of this and the metabolic fate so what is what comes under ketogenic and what comes under glucogenic at what comes under both so ketogenic or lysine and leucine whereas both is tryptophan threonine phenylalanine tyrosine and isoleucine whereas glucogenic comes like all the others comes with glucogenic so this is the metabolic fate okay so this is important non-protein amino acids with their respective functions so even if you have knowledge regarding this well and good or is just give a glance to it okay so just give a quick glance to it okay so next this there is a process called as transamination and de-amination okay which is again quite important so if you see this chart it is pretty clear and self-explanatory okay so transamination there is trans-amination that is transfer of amino group one from an amino acid to a keto acid so that is called as a transamination okay and it is again mediated by the so called enzymes which are nothing but the transaminases which are previously were called as a amino transferases okay so very important all amino acids except lysine threonine proline and hydroxyplorin participate in transamination so except these four all the others participate okay so these are the important points and only two namely aspartate transaminase and alan and transaminase make a significant contribution to the transamination okay so these are the enzymes and what all amino acids accept like exceptions are quite important right so make the note of it next oxidative d amination where is there is liberation of free ammonia coupled with oxygen so from the amine group there is liberation of the free ammonia okay so in the process of transamination so we have discussed right so there is amino i mean the transfer occurs but in oxidative deamination there is finally liberation of the free ammonia so the glutamate is only amino acid that undergoes oxidative deamination to significantly release or liberate free ammonia for urea synthesis so even in the previous chart if you see i see this is a glutamate right so glutamate undergoes oxidative demination in order to liberate free ammonia so as to participate in urea synthesis okay and glutamate dehydrogenase is a zinc containing mitochondrial enzyme okay so these are the important points so even you can have a look of this next non-oxidative deamination examples so here it's quite pretty clear so what are all the examples for non-oxidative deamination so just make a note of all these ok all the important points point to be noted are all these points so just give a glance to all these important points which are being noted here next we will discuss one by one so glycine this is the overview of glycine metabolism okay so so main thing related to glycine which is quite important is a metabolic disorders of glycine so that is glycineuria and primary hyperoxaluria okay so this is very important because they can ask us applied aspects okay so where the gla if you see glycine urea there is serum glycine concentration is normal but very high amount of it is being excreted in urine so urea means it has been excreted in urine it is because of defective renal reabsorption when there is defective renal reabsorption glycine urea occurs and it is characterized by increased tendency of formation of oxalate renal stones okay whereas the urinary oxalate level is normal in this patient so these are the true or false statements that can be asked so give a glance to it next primary hyperloxal urea so here there is increased urinary oxalate resulting resulting in oxalate stones okay so here there is oxalate stones okay so this is regarding that so primary is hypoxaleria is due to the defect in glycine transminase okay so it was asked once so what it is because of what it is because of defecting glycine transaminase next coming to the creatinine okay so just give a chat look to the metabolism of the creatine so it's pretty clear what are the reactions that occur so just give a look to this okay so the creatine is again converted to creatine phosphate okay so just have a look of this next phenyl phenylene and tyrosine so very very important so this chart is very very important okay and also the synthesis of phenylalanine is also important so sorry synthesis of tyrosine from phenylalanine okay so that is quite important so if there is a block here then it results in phenylkit ketone urea okay so phenylalanine and tyrosine are interrelated to each other so just give a good grip or just have a good glance to this chart okay have a grip of the metabolism related to both these so if you see here next is the thyrosin so tyrosine is actually important for the thyroid synthesis of thyroid hormones so okay and albinism is due to the lack of synthesis of melanin and it is a autosomal recessive disorder okay so tyrosine again important for melanin pigmentation and melanin i mean synthesis of pigment of melanin also so if there is a problem with tyrosine obviously it can result in lack of this pigment that is melanin okay so how it is being sick produced it's pretty clearly given in this chart so just have a look of that as well okay so these are the various catecholamines biosynthesis so phenylalanine converted to tyrosine that is converted to l dopa to dopamine to norepinephrine and epinephrine so the series of reactions and the enzymes involved quite important okay so next disorders of tyrosine metabolism the very very important area according to me is this ok yes you need to have an idea of the i mean the metabolism the chart and the series of reactions but the disorders related to them is the applied aspect so that's the reason they play like they take a more important i feel so just have a look of all the disorders related to tyrosine metabolism so exactly how the question can be asked is which enzyme is being blocked or what reaction is being affected in phenylketonuria then you have to go for this that is phenolinin hydroxylase okay so all these diseases and the respective enzymes and the respective reactions are quite important even alkeptonuria is again quite important so do give a good glance to this okay so next coming to the tryptophan so tryptophan so if you see this is the overview of tryptophan okay so hat nups disease okay it is characterized by low plasma levels of tryptophan and other neutral amino acids and their elevated urinary excretion okay so this is regarding tryptophan which is quite important for the nad okay so that is nicotinic acid ribonucleotide antinucleotide so so just have a look of this just give a glance no need to get into each and everything for this just what exactly is the importance of that okay so if you see they are important tryptophan is necessary for the coenzymes of niacin right so they can ask you where all the what is uh important amino acid for the coenzymes of niacin then you have to go for tryptophan okay so like that it's quite important next this is a serotonin melatonin pathway so melanin is different from melatonin okay so melanin is related to tyrosine now it is melatonin which is related to the tryptophan again okay so that is different so it is involved melatonin is involved in circadian rhythms right so this is quite important so have a look of this as well next system so this is a metabolism so i mean the sulfur containing amino acids is a system right so this is the overall view of it okay next the branch amino acids so marple syrup maple syrup maple syrup urine disease okay so this is a metabolic disorder of a branch chain amino acids okay so here the urine smells to be like a maple syrup or a burnt sugar hence the name is given like that okay so this is due to the defect in the enzyme branch of chain alpha keto acid dehydrogenase even that is quite important have a look next lysin cartilage plays a very important role in fatty acid oxidation okay so this is just a summary of lysine metabolism and cartilage so just the series of this so have a look of this just give a glance to it glutathione okay so glutathione is a tripeptide that contains glutamate okay next acetyl n-acetyl glutamate and aminobutyric acid so again these are very important so glutamate is decarboxylated to gaba which is present mostly in the brain so this is an important line again and glutamate is also present in clotting factors two seven nine and ten as gamma carboxy glutamate and it is again involved in coagulation so which of the following in gets involved in coagulation then you have to go for glutamate so glutathione is a tripeptide which contains glutamate okay so just give a glance to it next serine the over review of the sarin metabolism just have an idea so synthesis of essential non-essential amino acids so this really gives so what ah the non-essential amino acids and what from where are they synthesized from so this gives you the brief review of everything next the urea cycle everything kept in one chart all the important points a urea cycle mainly occurs in the liver and the urea is being eliminated by the kidney okay so this fumarate forms the link with the tca cycle next urea cycle is also called as ornithine cycle or creps henselt cycle and the enzymes which are present in mitochondria that is carbonyl phosphatase and ornithine trans uh trans carbomylase whereas enzymes which are present in cytosol are argino succinates agnostic synthase and arginase okay so many times the questions are asked in and around this particular flow chart or the urea cycle the cycle which is particularly given here so just i think you are very well aware of it so these are the various questions of the various important areas so arjuna's is activated by carbon dioxide and manganese and ornithine and lysine compete with arginine by competitive inhibition okay arginase is mostly found in the liver so all these are just the important points taken from your textbook note them down then the disease is related okay so what enzyme deficiency causes what or the which respective disease so hyper ammonia type one is because of deficiency of carbonyl phosphate synthesis one deficiency of ornithine trans carbamil is hyper ammonia type 2 adreno succinate synthesis deficiency causes citrullinemia okay citrulline anemia next argeno succinate enzyme deficiency causes argenosuccinic acid urine arginase defect or deficiency causes hyperagineemia okay so again this is quite important so everything related to urea cycle is put forward here have a look so here the atps and all that okay so that's it regarding urea cycle so with this we have given a very quick glance to the protein metabolism okay and the urea cycle so important areas are the diseases related to the respective amino acids and the little glands of the metabolism of the various amino acids and very important area is the urea cycle and what are the essential and non-essential amino acids and the names of the amino acids and the classification of the amino acids so that's enough so just have a look of this okay so this is regarding the quick revision of the protein metabolism okay thank you