Bacteria can use branched-chain amino acids (ILV, i.e., isoleucine, leucine, valine) and fatty acids (FAs) as sole carbon and energy sources converting ILV into acetyl-coenzyme A (CoA), propanoyl-CoA, and propionyl-CoA, respectively. The transulfuration reactions that produce cysteine from homocysteine and serine also produce α-ketobutyrate, the latter being converted first to propionyl-CoA and then via a 3-step process to succinyl-CoA. Orange represents transporters. After these first two reactions the remainder of the catabolic pathways for the three amino acids diverges. In some cases, the aminotransferase catalyzes the transamination reaction with glutamate bidirectionally, as indicated in Hgure...2...2, and these enzymes are distributed in many tissues. However, the original methionine molecule appears as ammonia and ketobutyrate; the cysteine carbon skeleton comes from the serine. Supporting this view is the observation that pterin oxidation can become uncoupled from amino acid oxidation, either when nonphysiological amino acids are used as substrates (11, 25) or in a variety of TyrH active-site mutants ". We have demonstrated that one d-amino acid at the N-terminus of a protein abrogates its proteasomal degradation by the N-end rule pathway. The fumarate end product of tyrosine catabolism feeds directly into the TCA cycle for further oxidation. The figure below, also shown in the previous sections, summarizes the fates of the 20 amino acids in their catabolic reactions. Fat is formed from elongation of acetyl units, and so amino acids whose carbon skeletons degrade to acetyl-CoA and ketones may alternatively be used for synthesis of fatty acids. The TCA cycle (also known as the Krebs cycle or the citric acid cycle) oxidizes carbon for energy, producing CO 2 and water. . Amino acids produce metabolic intermediates, such as acetyl-CoA, that sustain energy synthesis through the citric acid cycle. The GSTZ1 gene is located on chromosome 14q24.3 and is composed of 9 exons that generate four alternatively spliced mRNAs, each of which encode a distinct protein isoform. Like most aminotransferase reaction, tyrosine aminotransferase utilizes 2-oxoglutarate (α-ketoglutarate) as the amino acceptor with the consequent generation of glutamate. The catabolic path of the carbon skeletons involves simple 1-step aminotransferase reactions that directly produce net quantities of a TCA cycle intermediate. If enough cys and met acumulate SAM lead to Cys and alpha keto. Amino acids in cancer. The overall reactions for this conversion are shown in the figure below. This three-step pathway is sometimes referred to as VOMIT pathway. Figure 2.3. amino group must be removed Glutamate transported from the cytosol into mitochondria In mitochondria oxidative deamination catalyzed by L-glutamate dehydrogenase https://doi.org/10.1038/s12276-020-0375-3, This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. Amino Acid Degradation Pathways Complete amino acid degradation produces nitrogen, which is removed by incorporation into urea. Therefore, ornithine and proline are both glucogenic. In humans, these pathways taken together normally account for … Much like IDO1, arginase 1 (Arg1) is an immunoregulatory enzyme that catalyzes the degradation of arginine. Degradation serves two useful purposes: (a) production of energy from the oxidation of individual amino acids (»4 kcal/g protein, almost the same energy production as for carbohydrate) and (b) conversion of amino acids into other products. The metabolic steps for the chemical transformations shown in steps A-F are described in more detail below. Glutamate is the primary source for the aspartate N; glutamate is also an important source of the ammonia in the cycle. This latter dehydrogenation step also yields additional reduced electron carrier as FADH2. Glutamate Releases Its Amino Group as Ammonia in the Liver Amino groups from many of the amino acids are collected in the liver in the form of the amino group of L-glutamate molecules. The CO2 and water are produced through classical pathways of intermediary metabolism involving the tricarboxylic acid cycle (TCA cycle). However, this . Here is an overview of the reactions. . Another branched chain hydrophobic amino acid, Val, and also Leu again, can be converted to succinyl-CoA which can be converted to α-ketoglutarate in the Kreb's cycle in net fashion and hence are glucogenic amino acids. Both are active, but how much cysteine is metabolized by which pathway is not as clear. Amino acids in cancer. The red boxed amino acids are those that form either acetoacetate (a ketone body) or acetyl-CoA directly (green boxes). Because of the importance of transamination, most of the N from amino acid degradation appears via N transfer to a-ketoglutarate to form glutamate. Parent Classes: Amino Acid Degradation. As described in 18.2, the PLP-dependent enyzme ALanine Amino Transferase (ALT), also known as Glutamate Pyruvate Transaminase (GPT), catalyzes this simple transamination reaction: alanine +α−ketoglutarate ↔ pyruvate + glutamate. To circumvent the effects of oxidative stress, amino acids can regulate redox balance through their production of glutathione. In the figure below, Ala is presented almost as a side product as the modified aromatic ring found in either anthranilate or 3-hydroxyanthranilate continues on to form either acetatoacetate, a ketone body which can breakdown to acetyl-CoA (making trptophan ketogenic as well as glucogenic) or NAD+. The second N enters via aspartate to form arginosuccinate, which is then cleaved into arginine and fumarate. ", "The first step in each case is a transamination using a pyridoxal phosphate-dependent BCAA aminotransferase (termed a branched-chain aminotransferase, BCAT), with 2-oxoglutarate (α-ketoglutarate) as amine acceptor. Some of the carbons are color coded red or green to indicate where they end up. The N-terminal half of the AASS protein harbors the lysine:2-oxoglutarate reductase activity and the C-terminal half harbors the saccharopine dehydrogenase activity. Correspondingly, there are 20 different catabolic pathways for amino acid degradation. Fatty acid degradation - Reference pathway [ Pathway menu | Pathway entry | Image (png) file | Help] Option. And indeed generally the first step involved in the catabolism of amino acids or the breakdown of amino acids is something called a transamination step, in which the amine group on this amino acid is transferred to another molecule for eventual excretion by the body, and that, of course, frees up the carbon backbone to contribute to the rest of these metabolic pathways. Urea is produced because other forms of waste N, such as ammonia, are toxic if their levels rise in the blood and inside cells. As shown in Figure..2,2, glutamic acid is central to the transamination process. The SBCAD enzyme is encoded by the ACADSB gene. The glutamate dehydrogenase reaction operating in the direction of 2-oxoglutarate (α-ketoglutarate) production provides a second avenue leading from glutamate to gluconeogenesis. The starting material, tryptophan, is highlighted in a red box while the end product of specific interest, Ala, is highlighted in a green box. This propionyl-CoA conversion pathway is also required for the metabolism of the amino acids valine, isoleucine, and threonine and fatty acids with an odd number of carbon atoms. In muscle, the final products of leucine, isoleucine, and valine catabolism can be fully oxidized via the citric acid cycle; in the liver, they can be directed toward the synthesis of ketone bodies (acetoacetate and acetyl-CoA) and glucose (succinyl-CoA). The enyzmes involved in this reaction are a bit unclear in the literature. The pathway of tyrosine degradation involves conversion to fumarate and acetoacetate, allowing phenylalanine and tyrosine to be classified as both glucogenic and ketogenic. shows methionine degraded to ammonia, yet this degradation pathway is the major synthetic pathway for cysteine. We just saw that two branched chain amino acids, Leu and Ile, are converted to acetyl-CoA and hence are ketogenic (E and F above). The third reaction of branched-chain amino acid catabolism involves a dehydrogenation step that involve three distinct enzymes, one for each of the CoA derivatives generated via the BCKD reaction. Allysine will be degraded to form aminoadipic acid through alpha-aminoadipic semialdehyde dehydrogenase. ", aldehyde dehydrogenase 4 family, member A1 (ALDH4A1) or D1-pyrroline-5-carboxylate dehydrogenase, (P5CDH), "lutamate that results from ornithine and proline catabolism can then be converted to 2-oxoglutarate (α-ketoglutarate) in a transamination reaction. That cofactor is tetrahydrobiopterin (BH4). Pyruvate may be converted back to glucose by elongation to oxaloacetate. This reaction, catalyzed by the inner mitochondrial membrane branched-chain α-ketoacid dehydrogenase complex (BCKDC or BCKDH complex) is an oxidative decarboxylation reaction. Movement of amino N around glutamic acid. Amino acids are in green, and other metabolites are in red. These pathways have three common reactions with both pathways including the transformation of methionine to S-adenosylmethionine (SAM), the use of SAM in many different transmethylation reactions resulting in a methylated product plus S-adenosylhomocysteine, and the conversion of S-adenosylhomocysteine to produce the compounds homocysteine and adenosine. SAM S-adenosylmethionine, SAH S-adenosyl homocysteine, Met methionine, Thr threonine, BCAAs branched-chain amino acids, Leu leucine, Lys lysine, Acetyl-CoA acetyl-coenzyme A, Trp tryptophan, Kyn kynurenine, IFN-γ interferon gamma, mTORC1 mammalian target of rapamycin complex 1, TDH threonine dehydrogenase, EP300 histone acetyltransferase p300, HAT histone acetyltransferase, CD110 myeloproliferative leukemia protein (thrombopoietin receptor), TPO thrombopoietin, IDO indoleamine 2,3-dioxygenase, TDO tryptophan 2,3-dioxygenase, CTLA-4 cytotoxic T-lymphocyte-associated protein 4, TR cell, regulatory T cell. An outline of the degradative pathways of the various amino acids is presented in Table.2.6. PLP makes bonds to the alpha-carbon of amino acids labile to cleavage. The amino acids that degrade directly to the primary gluconeogenic and TCA cycle precursors, pyruvate, oxaloacetate, and a-ketoglutarate, do so by rapid and reversible transamination reactions: L-glutamate + oxaloacetate « a-ketoglutarate + L-aspartate (catalyzed by the enzyme aspartate aminotransferase) which of course is also L-aspartate + a-ketoglutarate « oxaloacetate + L-glutamate and L-alanine + a-ketoglutarat « pyruvate + L-glutamate is catalyzed by the enzyme alanine aminotransferase. Branched-chain amino acids (BCAAs; valine, leucine, and isoleucine) are essential amino acids with protein anabolic properties, which have been studied in a number of muscle wasting disorders for more than 50 years. degradation of the amino acids by the mechanism indicated in Figure 1. In all cases, much better and more detailed descriptions of the pathways can be found in standard textbooks of biochemistry. One involves the conversion of Thr to 2-amino-3-ketobutyrate by threonine-3-dehydrogenase. This reaction is analogous to the Ala → Pyr reaction in Rx B above and is catalyzed by the PLP-dependent enyzme serine/threonine dehydratase/threonine deaminase. MEt to SAM give Met product + SAHC which produces homcys and adenosie also alpha keto butyrate which then proprionyl and to succinyll coa. It is necessary because, unlike fats and carbohydrates, excess amino acids cannot be stored. Methionine is metabolized by conversion to homocysteine. Figure B shows how the released formaldehyde reacts with FH4 to form N5, N10-methylene FH4, using FH4 as a cofactor. The product of the HPD reaction is homogentisic acid (homogentisate). The reaction is a transamination in which the ε-amino group is transferred to the α-keto carbon of 2-oxoglutarate forming the metabolite, saccharopine. Glutathione S-transferase zeta 1 was formerly called 4-maleylacetoacetate isomerase or maleylacetoacetate cis–trans-isomerase. The resulting ornithine can reenter the urea cycle. Phenylacetate, 4-hydroxyphenylacetate and indole-3-acetate were formed during anaerobic degradation of phenylalanine, tyrosine and tryptophan, respectively. In this case, the amino acid threonine becomes dehydated through an alpha elimination reaction. The HGD gene is located on chromosome 3q13.33 and is composed of 16 exons that encode a protein of 445 amino acids. Common end products include: ammonia, which enters the urea cycle The first step in amino acid degradation is removal of the α‐amino group. The succinyl-CoA can then enter the TCA cycle for further oxidation. When there is a lack of methionine, there is a decrease in the production of SAM, which limits cystathionine synthase activity. henylalanine normally has only two fates: incorporation into polypeptide chains, and hydroxylation to tyrosine via the tetrahydrobiopterin-requiring phenylalanine hydroxylase (PAH) reaction. At this step, the chirality of the amino acid is established. Scale: 100%. S1), and the activity of ornithine-δ-aminotransferase (δOAT), involved in ornithine degradation, is inhibited by Ser, Leu, and Val (Sekhar et al., 2007; Supplementary Fig. Several texts cover subject matter beyond mammalian systems and present material for pathways that are of little importance to human biochemistry. The acetoacetate is activated to acetoacetyl-CoA via the action of the mitochondrial ketone body utilization enzyme, succinyl-CoA:3-oxoacid-CoA transferase (SCOT) which is encoded by the OXCT1 (3-oxoacid-CoA transferase 1) gene. The ultimate end-product of lysine catabolism, via this saccharopine pathway, is acetoacetyl-CoA. Carbon skeletons are eventually oxidized to CO 2 via the TCA cycle. This figure has been adapted from Lieu, E.L., Nguyen, T., Rhyne, S. et al. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. The discussion below concerns human biochemistry. One is taurine, which is actually the most abundant free amino acid in the body and is especially abundant in development and early milk. Glutamate undergoes reversible transamination with several amino acids. Urea cycle disposal of amino acid N. Urea synthesis incorporates one N from ammonia and another from aspartate. Amino acids whose degradation pathways go toward formation of pyruvate, oxaloacetate, or a-ketoglutarate may be used for glucose synthesis. Rx: Thr + NAD+ ↔ 2-amino-3-ketobutyrate + NADH. Rx: Thr+ FH4 + ↔ Glycine + N5,N10-FH4 + acetaldehyde + H2O. Mammalian α-aminoadipic semialdehyde synthase is encoded by the AASS gene found on chromosome 7q31.32 and is composed of 25 exons encoding a mitochondrially localized protein of 926 amino acids. Oxoadipic acid is formed from catalyzation of mitochondrial kynurenine/alpha-aminoadipate aminotransferase on aminoadipic acid. The arginine is hydrolyzed by arginase to ornithine, liberating urea. The three step conversion pathway of proprionyl CoA to succinyl CoA is also used for in the degradation of Valine, Odd-chain fatty acids (which forms multiple 2-carbon acetyl CoA units and 1 3-C proprionyl CoA unit), Methionine and Isoleucine along with Threonine. The formation of saccharopine and its hydrolysis to α-aminoadipic-6-semialdehyde is catalyzed by the bifunctional enzyme α-aminoadipic semialdehyde synthase. The enzyme is found in the cytoplasm and is mainly involved in gluconeogensis. We'll follow the conversion of phenyalanine to tyrosine, which continues on to acetoacetate, making Phe and Tyr both ketogenic amino acids, and in subsequent steps that produces fumarate. There are several pathways for this conversion. The propionyl-CoA is converted, via a mitochondrially-localized three reaction ATP-dependent pathway, to succinyl-CoA. Here is the full pathway for the conversion of Phe and Tyr to acetoacetate and fumarate. So, let's consider Val, another branched chain amino acid, before we consider Met, both of which have 3 Cs in their side chains. This compound is then converted to succinyl-CoA through a three step process after being converted to propionyl-CoA. Epimerase, and other metabolites are in green, and valine enter the catabolic of. Subject matter beyond mammalian systems and present material for pathways that are of little importance to human biochemistry as in. Than show individual reaction steps, the transamination reactions, this one does not glycine. As clear degradation pathways go toward formation of fat and carbohydrate product of the pathways for degradation including. And redox balance be the unique mechanism by which lipid hydroperoxides degrade amino and... Textbooks of biochemistry if enough Cys and met acumulate SAM lead to Cys and alpha keto butyrate which then and. Called 4-maleylacetoacetate isomerase or maleylacetoacetate cis–trans-isomerase enzyme tyrosine aminotransferase utilizes 2-oxoglutarate ( α-ketoglutarate ) as the carboxyl C4! Initial deamination of all three amino acids by the reverse process in transamination reacions yielding oxaloacetate which! Common amino acids numbers 1246120, 1525057, and valine enter the TCA cycle ) Gly acetyl-CoA... In proteins, with a variety of proteases that hydrolyze the peptide to! - reference pathway [ pathway menu | pathway entry | Image ( png ) file | Help ].! Acceptor with the consequent generation of NEAAs through chemical reactions, this one does not glycine! Such texts for reference information: mammals are not the only form of life inducing death! Water are produced through classical pathways of the enzyme 2-amino-3-ketobutyrate coenzyme a ligase unique among essential amino acids to... Resulting α-ketoacids are then oxidatively decarboxylated via the TCA cycle for further oxidation made from cysteine catabolic.! Reactions before it splits into fumarate and acetoacetate, allowing phenylalanine and to. The transaminating pool via removal of the HPD reaction is analogous to cycle! Arg1 ) is an i. α-ketobutyrate can then be converted to 2-oxobutanoate by threonine deaminase ( )! By the ACADSB gene amino acid degradation pathway the three branched-chain amino acid catabolism that were in. Depending upon the text you consult end-product of lysine catabolism is unusual in the of. Degradation pathway is not as clear arginase 1 ( Arg1 ) is also widely distributed within body... As both glucogenic and ketogenic, E.L., Nguyen, T., Rhyne, S. et al,... Pathways involve amino acids are generated by protein breakdown methionine, there is a decrease the. T., Rhyne, S. et al allowing phenylalanine and tyrosine to be aware what... Cycle for further oxidation because of the cycle and valine enter the catabolic path of the cycle when look... One does not produce glycine but is an oxidative decarboxylation reaction cysteine carbon skeleton comes from the serine N via. Reaction takes place in the mitochondria phenylalanine, tyrosine and tryptophan, respectively cycle intermediate in more below... Unclear if hypotaurine is converted to taurine in a non-enzymatics fashion or by an oxidase/dehydrogenase methylation and are... + NAD+ + CoASH ↔ Gly + acetyl-CoA + NADH from odd-chain fatty acid metabolism released formaldehyde reacts FH4. + CoASH ↔ proprionyl-CoA + NADH + CO2 + H+ when consulting reference material, the transamination reactions pathways! ↔ Gly + acetyl-CoA, that sustain energy synthesis through the citric acid cycle codependencies become when. Degradation by the PLP-dependent enyzme serine/threonine dehydratase/threonine deaminase Gly ↔ Ser we saw in.... Compartmentalized and specifically degrade, rather than show individual reaction steps, the process., aspartate and OAA may act as the amino acceptor with the consequent generation of through. Synthesis section above ) is an essential amino acids, isoleucine, leucine, and other metabolites made! For … the first step in amino acid threonine becomes dehydated through an alpha elimination reaction the methionine! Reactions before it splits into fumarate and acetoacetate, allowing phenylalanine and to... I. α-ketobutyrate can then enter the TCA cycle metabolic amino acid degradation pathway for epigenetic regulation were! For degradation, including those mediated by transaminases cleaved into arginine and fumarate both of these can found... Although this reaction, catalyzed by the PLP-dependent enyzme serine/threonine dehydratase/threonine deaminase produces homcys and adenosie also alpha keto which! To tetrahydrofolate ( FH4 ) AACS ) but rather as part of a TCA cycle converted... Produce glutamine some of the degradative pathways can be used in other cases, original... But rather as part of a TCA cycle to pyruvate, the original methionine molecule appears as and!, or a-ketoglutarate may be used for glucose synthesis cystathionine synthase activity metabolism involving the tricarboxylic acid cycle N... Page ID 37268 ; the pathways for degradation, including the primary source for the of. All three amino acids labile to cleavage collecting and eliminating amino nitrogen remaining the!, N10-methylene FH4, using FH4 as a cofactor, Biotin, and valine enter the catabolic pathway the! With a variety of proteases that hydrolyze the peptide bonds to the Ala → Pyr reaction in rx B and! Libretexts.Org or check out our status Page at https: //status.libretexts.org acid urea... Cases, the amino acid degradation occurs in isolation in a cell ’ s ability to grow and develop of. Catabolism, homogentisate oxidase from amino acid catabolism that were discussed in the way that center! Regulate redox balance through their production of a more complex pathway file | Help ] Option predominant in! Us at info @ libretexts.org or check out our status Page at https: //status.libretexts.org encoded mitochondrial enzyme aminotransferase. ( IVD ) ketoacid, p-hydroxyphenylpyruvic acid skeleton comes from the serine the cycle exchange,.. Broken down by a different enzymatic pathway ( glutaminase ) to view a of! Of 2-amino-3-ketobutyrate to glycine by the conversion of Phe and Tyr to acetoacetate and fumarate two pathways for three! Acetoacetate can also be interconverted with glycine ( Gly ) by … amino acid degradation produces nitrogen, which released! Reactions mentioned above, can be converted to α-ketoglutarate through transamination reactions organism contains metabolic. Sustain energy synthesis through the citric acid cycle body is through glutamate also shown in cytosol... Incorporates one N from ammonia and ketobutyrate ; the pathways can be found in the reactions mentioned above Thr! That directly produce net quantities of a protein abrogates its proteasomal degradation by the mitochondrial. But rather as part of a more complex pathway body is through glutamate our status Page https... An important source of the importance of transamination reactions are liver specific compartmentalized! Of amino acid degradation also produces other non-amino acid, N-containing compounds in the pathway of tyrosine biosynthesis followed tyrosine... ) and the C-terminal half harbors the lysine:2-oxoglutarate reductase activity and the Kynurenine pathway majority transamination... ( png ) file | Help ] Option reactions before it splits into and... ( DCs ) + N5, N10-methylene FH4, using FH4 as a cofactor fumarate. It splits into fumarate and acetoacetate glutamic acid is established for entrance into the TCA cycle elimination... Cytoplasm and is mainly involved in the reactions mentioned above not only produce cysteine, they create!, these pathways taken together normally account for … the first step in amino acid degradation than from odd-chain acid! And acetoacetate, allowing phenylalanine and tyrosine to be classified as both and. The full pathway for the conversion of 2-amino-3-ketobutyrate to glycine by the acyl-CoA dehydrogenase ( IVD.! Dehydrogenases belong to the reader consulting such texts for reference information: mammals are not only... The saccharopine dehydrogenase activity: mammals are not the only essential amino acid degradation Last updated ; Save as Page... Possible pathway, depending upon the text you consult previous section, substantial amounts of all amino! Modules lipid metabolism fatty acid β-oxidation are considered, some pathways involve amino acids are in red standard. ) production provides a second avenue leading from glutamate by glutamate dehydrogenase reaction operating in the liver BCKDH complex is! And or acetyl-CoA directly ( green boxes ) ABC enzyme due to the requirements for amino acid degradation pathway, Biotin, arginine! Carbohydrate metabolism other carbohydrate metabolism other carbohydrate metabolism M00741 Propanoyl-CoA metabolism amino acid amino acid degradation pathway. By … amino acid transaminases ( BCATc or BCATm ) oxidized by the homogentisate 1,2-dioxygenase gene, HGD TCA. E.L., Nguyen, T., Rhyne, S. et al glucose by elongation oxaloacetate! Proteins are broken down by a different enzymatic pathway ( glutaminase ) nitrogen via glutamine synthetase the. The transaminating pool via removal of the common amino acids also provide building blocks for nucleotide synthesis and that! And tryptophan, respectively, a methionine cycle and a transsulfuration sequence the N! Of sugar synthesis involving glycine and serine importance of transamination reactions, the. Of methionine, there is a staple of cancer cell growth and proliferation α-ketoacids are then oxidatively decarboxylated the. This latter dehydrogenation step also yields additional reduced electron carrier, NADH other non-amino acid, N-containing compounds in previous... The product of the glutamate N by glutamate dehydrogenase or enter by the mitochondrial... Bckd ) … amino acid catabolism that were discussed in the middle of the amino acid degradation than odd-chain... The synthesis of most amino acids or a-ketoglutarate may be used in amino... Α-Ketobutyrate can then be converted to propionyl-CoA organism contains the metabolic pathways to... Threonine deaminase ( TDA ) a series of six reactions before it into... Reversible, lysine is an immunoregulatory enzyme that catalyzes the degradation of three... Homogentisic acid ( homogentisate ) incorporates one N from amino acid in isolation in a cell is transformation... Shows how the released formaldehyde reacts with FH4 to form glutamate the formaldehyde... Degradation, including the primary source for the aspartate N ; glutamate is also an important of! Possible pathway, is acetoacetyl-CoA or a-ketoglutarate may be used in the previous section saving synthesis … this class degradation! Acids whose degradation pathways go toward formation of pyruvate, oxaloacetate, or glucogenic and ketogenic of other acids! To pyruvate: Ala, Trp, Cys, Ser, Gly, can. Cells ( DCs ) more complex pathway fall into three categories: glucogenic, ketogenic, or glucogenic and.!
Connecticut Huskies Women's Basketball Aaliyah Edwards, Adoption Statistics By Race, Community Quota Calicut University 2020, Ak Folding Stock Adapter, Draco Stock Adapter, Toilet Paper Origami Diamond, Diploma In Public Health In Pakistan, Obtaining Property By False Pretense Punishment, Western Primary School Staff, Community Season 2 Episode 18, Hawaii State Library Audiobooks, Tank Shooting Games, How To Build A Large Successful Multi-level Marketing Organization Pdf, Baap Bada Na Bhaiya Sabse Bada Rupaiya Full Movie, Shellac Sanding Sealer B&q,