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Proteinogenic amino acids are amino acids that are precursors to proteins, and are incorporated into proteins during translation.[1] Throughout known life, there are 23 proteinogenic amino acids,[citation needed] 20 in the standard genetic code and an additional 3 that can be incorporated by special translation mechanisms. In contrast, non-proteinogenic amino acids are either not incorporated in proteins (like GABA, L-DOPA, or triiodothyronine), or are not produced directly and in isolation by standard cellular machinery (like hydroxyproline and selenomethionine). The proteinogenic amino acids have been found to be related to the set of amino acids that can be recognized by ribozyme autoaminoacylation systems.[2] Thus, nonproteinogenic amino acids would have been excluded by the contingent evolutionary success of nucleotide-based life forms.
Nonproteinogenic amino acids are incorporated in nonribosomal peptides, which are not produced by the ribosome during translation. The following illustrates the structures and abbreviations of the 21 amino acids that are directly encoded for protein synthesis by the genetic code of eukaryotes. In addition, the symbol X is used to indicate an amino acid that is completely unidentified. Following is a table listing the one-letter symbols, the three-letter symbols, and the chemical properties of the side chains of the standard amino acids. Note: The pKa values of amino acids are typically slightly different when the amino acid is inside a protein.
In mass spectrometry of peptides and proteins, knowledge of the masses of the residues is useful. The table below lists the abundance of amino acids in E.coli cells and the metabolic cost (ATP) for synthesis the amino acids. Very abundant and very versatile, it is more stiff than glycine, but small enough to pose only small steric limits for the protein conformation.
Asp behaves similarly to glutamic acid, and carries a hydrophilic acidic group with strong negative charge. Glu behaves similarly to aspartic acid, and has a longer, slightly more flexible side chain.
Essential for humans, phenylalanine, tyrosine, and tryptophan contain a large, rigid aromatic group on the side chain. Pro contains an unusual ring to the N-end amine group, which forces the CO-NH amide sequence into a fixed conformation. Tyr behaves similarly to phenylalanine (precursor to tyrosine) and tryptophan, and is a precursor of melanin, epinephrine, and thyroid hormones. Ketogenic, with the products not having the ability to form glucose: These products may still be used for ketogenesis or lipid synthesis. The proteinogenic set used by known life on Earth appears to be arbitrarily selected by evolution, according to current knowledge, from many hundreds of possible alpha-type amino acids.
An extremely economical choice, Bulkpowders Pure Whey matches Myprotein on price but beats them on taste, mixability and macronutrient comparison. It is incredibly cheap at just ?0.32 per serving (unflavoured) – however keep an eye on the delivery cost when ordering online. It is ever so slightly more expensive than Myprotein and Bulk Powders, but it is the outstanding quality of this product that sees it reach for 1st place on our list.
It is available in some really exciting flavours (is also available unflavoured) and mixes really well. It has also ranked as the joint most effective protein supplement with Optimum Gold Standard – but at half the price, there could only be one winner. As a logical first step, in order to get our whey protein comparison results we compared the type of protein used in all of the products. Price wise, we compared the prices on each product by working out the cost per 25g serving. PHD Pharma Whey was the most expensive product in the test at ?1.10 per serving (300% of the cheapest product).
There is a clear correlation here between the types of protein used and the price of the product, with the ‘budget’ products using whey protein concentrate and the ‘premium’ division (using isolate and hydrolysed) clearly visible – and The Protein Works Whey 90 sandwiched comfortably in between. As you’d expect, the ingredients were largely the same, but with a few variables (both positive and negative) in each product.
All three of the premium products contain artificial flavourings and sweeteners, and do not offer unflavoured options. The Protein Works Whey 80 had the same base, but also included a patented system of digestive enzymes designed to increase absorption called Aminogen – an excellent addition in our eyes, bringing us back to the ‘you are what you digest’ comment earlier. Interesting comparisons can be drawn when comparing the macronutrient values of each product. As you can see from the table above, The Protein Works Whey 90 contains the best ratio of protein to carbs and fats, and it is also the lowest calorie choice. Interestingly, the highest price product, PHD, contains the lowest amount of protein and the highest amount of carbohydrates.
When the taste was compared, the most popular was Bulkpowders, closely followed by The Protein Works (both products).
PHD and Optimum Gold Standard both scored well on taste and mixability, with PHD generally considered slightly better tasting but slightly less mixable. Finally, and crucially, we also scored each product based on its effectiveness for its users.
The remainder of protein digestion occurs within the duodenum and jejunum of the small intestine.
Trypsin then cleaves more trypsinogen to trypsin, as well as chymotrypsinogen, proelastase, and procarboxypeptidases to their active forms. Intestinal uptake of peptides involves H+ co-transporters which are also members of the SLC family.
SLC6A19 is responsible for the transport of neutral amino acids in a Na+-dependent transport reaction.
The lack of intestinal tryptophan transport is responsible for most, if not all, clinical phenotypes of Hartnup disorder.
Symptoms of Hartnup disorder may begin in infancy or early childhood, but sometimes they begin as late as early adulthood. S-adenosylhomocysteine is then cleaved by adenosylhomocyteinase (also called S-adenosylhomocysteine hydrolase) to yield homocysteine and adenosine. Homocysteine can be converted back to methionine by methionine synthase (also called homocysteine methyltransferase).
The nature of the lens dislocation (subluxation), evident in homocysteinemia patients, can serve as a differential diagnostic tool.
Homocysteinemia can also result from vitamin deficiencies due to the role of the co-factor forms of B6, B12, and folate in the overall metabolism of methionine. Indeed, the measurement of serum methionine and methylmalonic acid in cases of homocysteinemia allows for a differential diagnosis of the nutritional (non-genetic) cause. Wilson disease, lead poisoning, and rheumatoid arthritis), and alpha-mercaptopropionylglycine, α-MPG (a second-generation chelating drug).
Untreated PKU leads to severe mental retardation, however, the precise mechanism by which this enzyme deficiency leads to the severe neural degeneration is not fully understood. The glutamate that results from ornithine and proline catabolism can then be converted to 2-oxoglutarate (α-ketoglutarate) in a transamination reaction.
Propionyl-CoA carboxylase functions as a heterodimeric enzyme and the two different subunits (alpha and beta) are encoded by two different genes, PCCA and PCCB. There are several pathways for non-protein disposition of cysteine that include both metabolism and catabolism. The metabolism of the branched-chain amino acids is critical to overall nitrogen homeostasis in the brain and to the maintenance of proper levels of the excitatory neurotransmitter, glutamate.
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Transport yourself to a tropical island and pump your body with protein, fiber, and antioxidants with our Coconut Mango Power Protein Shake. The Branched Chain Amino Acids are a group of 3 essential amino acids, specifically: leucine, isoleucine, and valine. Not only can BCAAs help optimize protein balance, but given their direct pathway to muscle cells, they act as an effective energy source during training. That’s why you should be taking them before an intense workout, and during a marathon sweat session. Ultimately, that helps increase overall training capacity and volume — it also makes the squats you did so much more bearable a day later. Both eukaryotes and prokaryotes can incorporate selenocysteine into their proteins via a nucleotide sequence known as a SECIS element, which directs the cell to translate a nearby UGA codon as selenocysteine (UGA is normally a stop codon). Proteinogenic amino acids can be condensed into a polypeptide (the subunit of a protein) through a process called translation (the second stage of protein biosynthesis, part of the overall process of gene expression).
Other reasons have been offered to explain why certain specific nonproteinogenic amino acids are not generally incorporated into proteins; for example, ornithine and homoserine cyclize against the peptide backbone and fragment the protein with relatively short half-lives, while others are toxic because they can be mistakenly incorporated into proteins, such as the arginine analog canavanine. The structures given below are standard chemical structures, not the typical zwitterion forms that exist in aqueous solutions. The masses listed are based on weighted averages of the elemental isotopes at their natural abundances.
Protein pKa calculations are sometimes used to calculate the change in the pKa value of an amino acid in this situation. Conditionally essential amino acids are not normally required in the diet, but must be supplied exogenously to specific populations that do not synthesize it in adequate amounts.
Negative numbers indicate the metabolic processes are energy favorable and do not cost net ATP of the cell.[4] The abundance of amino acids includes amino acids in free form and in polymerization form (proteins).
It behaves fairly neutrally, and can be located in both hydrophilic regions on the protein outside and the hydrophobic areas inside.
Under oxidizing conditions, two cysteines can join together in a disulfide bond to form the amino acid cystine. In even slightly acidic conditions, protonation of the nitrogen occurs, changing the properties of histidine and the polypeptide as a whole. Always the first amino acid to be incorporated into a protein, it is sometimes removed after translation. It can disrupt protein folding structures like I± helix or I? sheet, forcing the desired kink in the protein chain.
Used in proteins and as a storage for ammonia, it is the most abundant amino acid in the body. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes. Naturally fluorescent, its fluorescence is usually quenched by energy transfer to tryptophans. Xenobiology studies hypothetical life forms that could be constructed using alternative sets using expanded genetic codes. It contains the best macronutrient values of the group, and is ideal for those following a limited calorie diet. The ingredients are clean, it contains a patented absorption blend and is certified non GMO.

MyProtein Impact Whey, Bulkpowders Pure Whey and The Protein Works Whey Protein 80 all contained a base of whey protein concentrate. Interestingly, all of the ‘budget’ options seemed to contain the cleanest ingredient list; both MP Impact Whey and Bulkpowders were simply whey protein concentrate and soy lecithin (an emulsifier) – with various additions depending on the flavour. The Protein Works Whey 90 also had a clean ingredients list – just whey protein isolate and soy lecithin. Maximuscle Promax contains Taurine, whilst both PHD and Optimum Gold Standard contain a digestive enzyme blend, similar to that of The Protein Works Whey 80. One would expect the protein supplements containing whey protein isolate to have the best ratio of protein to calories, carbs and fat. The Protein Works Whey 80 also has an impressive breakdown, especially for a concentrate, and is comparable with Optimum Gold Standard despite being nearly half of the price.
One can only assume from these results that the additional ingredients in the likes of Maximuscle and PHD negatively impact the actual protein count. Bulkpowders didn’t have as wide a flavour range as the likes of MyProtein, but the general consensus was that the flavours they did have were highly enjoyable. The best feedback went to The Protein Works Whey 80 and Optimum Gold Standard Whey – both of which were considered highly effective.
The rest of the products were all considered marginally less effective, but still scored very well – apart from Maximuscle, who’s effectiveness received distinctly average reviews.
Adenosylhomocysteinase is encoded by the AHCY gene located on chromosome 20q11.22 and is composed of 17 exons that generate two alternatively spliced mRNAs encoding adenosylhomocysteinase isoform 1 (432 amino acids) and adenosylhomocysteinase isoform 2 (404 amino acids).
This reaction was also discussed in the context of vitamin B12-requiring enzymes in the Vitamins page.
The anemia develops due to the trapping of folate in the reduced form (N5-methyl-THF) which results in depletion of the active folate pool. The sulfur from the essential amino acid, methionine, is required for the synthesis of cysteine.
Lens dislocation is also found in patients suffering from Marfan syndrome, which is a connective tissue disorder caused by defects in the fibrillin gene (FBN1).
Vitamin B6 (as pyridoxal phosphate) is required for the activity of CBS and cystathionine γ-lyase and the homocysteinemia that results with B6 deficiency is also associated with elevated methionine levels in the blood. The enzyme methylmalonyl-CoA mutase also requires B12 and so a homocysteinuria resulting from a deficiency in this vitamin is also associated with methylmalonic academia. One theory suggests that the accumulation of phenylalanine interferes with the transport of tyrosine into the brain.
The PYCR1 gene is located on chromosome 17q25.3 and is composed of 9 exons that generate five alternatively spliced mRNAs that encode four different isoforms of the enzyme.
Glutamate serves as the precursor for the synthesis of both ornithine and proline which are derived from the Δ1-pyrroline-5-carboxylate intermediate in the pathway.
Indeed, the interconversion of serine and glycine via the involvement of THF represents the major pathway for the generation of N5,N10-methylene-THF which of a member of the active pool of folate derivatives. Serine can be derived from the glycolytic intermediate, 3-phosphoglycerate, in a three-step reaciton pathway. The glutamine synthetase enzyme is encoded by the glutamate-ammonia ligase gene (symbol: GLUL) which is located on chromosome 1q31 and is composed of 9 exons that generate several alternatively spliced mRNAs, each of which encode the same 373 amino acid protein.
The GLS2 encoded glutaminase is dependent on inorganic phosphate (Pi) for activity and is, therefore, also referred to as phosphate-activated glutaminase, PAG. Catabolism of Δ1-pyrroline-5-carboxylate back to glutamate is catalyzed by aldehyde dehydrogenase 4 family, member A1 (also called delta-1-pyrroline-5-carboxylate dehydrogenase, P5CDH). The catabolism of ornithine and proline is essentially a reversal of their synthesis from glutamate. The PCCA gene is located on chromosome 13q32 and is composed of 27 exons that generate three alternatively spliced mRNAs. The CDO1 gene is located on chromosome 5q23.2 and is composed of 6 exons that encode a 200 amino acid protein. The enzyme sulfite oxidase (gene symbol: SUOX) then catalyzes the conversion of sulfite to sulfate. Catabolism of cysteine is responsible for the release and or transfer of the sulfur from this amino acid. The other B12-requiring enzyme is methionine synthase (see the Cysteine Synthesis section above).
The BCAT1 gene is located on chromosome 12p12.1 and is composed of 13 exons that generate five alternatively spliced mRNAs, each of which encode a distinct isoform.
The critical enzymes that are necessary for this homeostatic process are the BCATc and BCATm isoforms of the BCAA aminotransferases.
The DLD gene encodes the same dihydrolipoamide dehydrogenase subunits found in the PDHc and the 2-oxoglutarate dehydrogenase complexes. The three branched-chain amino acids, isoleucine, leucine, and valine enter the catabolic pathway via the action of the same two enzymes.
The first reaction of tyrosine catabolism involves the nuclear genome encoded mitochondrial enzyme tyrosine aminotransferase and generates the corresponding ketoacid, p-hydroxyphenylpyruvic acid.
Use these 4 power post workout meals to refuel effectively and jack your body up with protein. The Maca Mint Chocolate Chip Protein Blizzard is an uber-lean, nutrition-packed, refreshing RUSH of lean, physique-chiseling, full-blown ab fuel. Those magical, mysterious letters are seemingly everywhere in the supplement universe; often plastered in vivid color on nearly every jug of protein powder, pre-workout, and amino acid-based recovery drink. They make up about 40% of the TOTAL amino acid content in the body—the largest of any group—with about 18% concentrated in muscle tissue.1 You already get an influx of BCAAs naturally from dietary protein sources and protein powder, but supplemental amounts can carry major benefits. While most amino acids are first broken down and processed by the liver, the BCAAs are unique in that they shuttle straight to muscle cells. Unless that protein balance stays at a net positive, you WILL lose muscle mass over time — and that’s why eating a waterfall of protein everyday is so critical.
For anyone who exercises religiously and trains like a beast, amino acid depletion and muscle breakdown happen naturally as a direct result of intense training. BCAA supplementation can help accelerate recovery (again, because the muscles are flooded with free amino acids) and significantly reduce post-workout soreness (DOMS).
For convenience, we’ve broken out the rankings into flavored powders, unflavored powders, and capsules. In some methanogenic prokaryotes, the UAG codon (normally a stop codon) can also be translated to pyrrolysine. Forming a peptide bond results in elimination of a molecule of water, so the mass of an amino acid unit within a protein chain is reduced by 18.01524 Da.
It binds to positively charged molecules and ions, and is often used in enzymes to fix the metal ion. Like isoleucine, leucine, and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. It is used by many proteins as a regulatory mechanism, changing the conformation and behavior of the polypeptide in acidic regions such as the late endosome or lysosome, enforcing conformation change in enzymes. Their molecules are rigid, and their mutual hydrophobic interactions are important for the correct folding of proteins, as these chains tend to be located inside of the protein molecule.
The flexibility of the chain makes lysine and arginine suitable for binding to molecules with many negative charges on their surfaces. Common in collagen, it often undergoes a post-translational modification to hydroxyproline.
Both are very hydrophilic, so the outer regions of soluble proteins tend to be rich with them.
Miller-type experiments on artificial abiogenesis show that alpha-type amino acids predominate in water-based 'primordial soups', but beta-type amino acids dominate when less water is present. However, it doesn’t taste quite as good as some of the other options, and does not contain an absorption blend to aid digestion. PHD contains added Glutamine and BCAA’s, however it also comes with a few questionable ingredients – Xanthan gum and Sodium Carboxymethylcellulose being the most notable. The Protein Works had an outlandish selection of flavours, including Butterscotch Ripple and Lemon Shortcake – all of which were very popular. Optimum Gold Standard Whey acknowledges this in the various awards it has won over the past few years, but The Protein Works Whey 80 is on a par with it, despite not being as well celebrated.
The methionine synthase reaction represents the clinically most significant of only two vitamin B12-requiring enzymes in human cells.
The active folate pool is required for purine and thymine nucleotide biosynthesis needed for DNA synthesis. The synthesis of cysteine represents an extremely important and clinically relevant biochemical pathway. Genetic defects are known for both the CBS gene (see next section) and the cystathionine γ-lyase gene. In homocysteinemia the lens subluxation occurs in a downward and inward direction, whereas in Marfan syndrome the lens subluxation occurs upward and outward.
The conversion of glutamate to Δ1-pyrroline-5-carboxylate is catalyzed by a bi-functional enzyme that is a member of the aldehyde dehydrogenase family.
Formation of Δ1-pyrroline-5-carboxylate occurs via the action of the bi-functional enzyme, aldehyde dehydrogenase 18 family, member A1 (also known as delta-1-pyrroline-5-carboxylate synthase). WBS is associated with multiple organ system involvement typically showing supravalvular aortic stenosis (SVAS), mental retardation, and distinctive facial features.
N5,N10-methylene-THF is required for purine nucleotide and thymine nucleotide biosynthesis. Asparagine synthetase is encoded by the ASNS gene which is located on chromosome 7q21.3 and is composed of 15 exons that generate several alternatively spliced mRNAs. The GLS2 gene is located on chromosome 12q13.3 and is composed of 19 exons that undergo alternative splicing to yield several mRNAs that encode four different isoforms of the enzyme. The dehydrogenase is encoded by the ALDH4A1 gene located on chromosome 1p36 and is composed of 17 exons that generate three alternativley spliced mRNAs, two of which encode the same protein.
The PRODH gene is located on chromosome 22q11.21 and is composed of 16 exons that generate two alternatively spliced mRNAs.
Since arginine is metabolized to urea and ornithine, and the resulting ornithine is a glucogenic precursor, arginine is also a glucogenic amino acid. Proline is oxidized back to Δ1-pyrroline-5-carboxylate via the action of proline dehydrogenase (PRODH).
Propionyl-CoA carboxylase is called an ABC enzyme due to the requirements for ATP, Biotin, and CO2 for the reaction. The PCCB gene is located on 3q21–q22 and is composed of 17 exons that generate two alternatively spliced mRNAs. The SUOX encoded enzyme is somewhat unique in that it uses the oxygen atom from H2O to convert sulfite to sulfate, (SO42–) and releases two protons (H+).
In addition to alternative splicing (generating two mRNAs), there are alternative in-frame translational start sites in the NFS1 derived mRNAs. Taurine synthesis occurs primarily in the liver since this is the only bile acid synthesizing tissue in the body However, taurine can be transported to the blood and disseminated to other tissues. The catabolism of cysteine can also involve a metabolic pathway as is the case for taurine synthesis. APS is then phosphorylated at the 3'-position of the ribose moiety forming the ultimate product, PAPS. This propionyl-CoA conversion pathway is also required for the metabolism of the amino acids valine, isoleucine, and threonine and odd-chain fatty acids.

The PCCB gene is located on chromosome 3q21–q22 and is composed of 17 exons that generate two alternatively spliced mRNAs.
The primary protein encoded by the BCAT1 gene is a cytosolic version of the enzyme and the protein is identified as BCATc. The initial deamination of all three amino acids is catalyzed by one of two branched-chain amino acid transaminases (BCATc or BCATm). This propionyl-CoA conversion pathway is often remembered by the mnemonic as the VOMIT pathway, where V stands for valine, O for odd-chain fatty acids, M for methionine, I for isoleucine, and T for threonine. It takes 5 minutes to make and it's jacked with protein, antioxidants, fiber, and nutrients. In the spirit of lean holiday indulgence, we've blended up The Peppermint Bark Protein Shake — an exact replica of the candy in lean, protein shake form. They actually have real, tangible benefits, and can provide a lift for anyone that trains regularly, including increased muscle growth, turbocharged endurance, improved body composition, and significantly reduced post-workout soreness — both for the casual lifter and seasoned vets alike. They’re a direct line of fuel, which has MAJOR perks — both on performance and muscle growth. In bacteria, the AUG initiation codon is translated to N-formylmethionine when it is actually used to initiate translation and translated normally (to methionine) at other times.
When located inside of the protein, aspartate and glutamate are usually paired with arginine and lysine. As too much flexibility is usually not desired, as a structural component, it is less common than alanine. This methyl group can be activated, and is used in many reactions where a new carbon atom is being added to another molecule.
Both alpha- and beta-based sets could form the basis for alternative protein constructions and life forms.
All three of the premium products contain artificial flavourings and sweeteners, and do not offer unflavoured options – so these are best avoided for those looking to stay away from unnecessary additives. Both Bulkpowders and The Protein Works received great feedback for their mixability as well, although The Protein Works 90 didn’t seem to mix as well as The Protein Works 80. The MAT enzymes encoded by the MAT1A gene function as either a homotetramer identified as MAT I (called the alpha form), or as a homodimer identifed as MAT III (called the beta form). Methionine synthase, in addition to B12, requires the folate-derived vitamin co-factor, N5-methyltetrahydrofolate (N5-methyl THF).
Bone marrow erythroblasts begin to enlarge in preparation for cell division but, due to loss of nucleotide synthesis, they remain as megaloblasts. Several vitamins are required for this metabolic pathway to proceed emphasizing the nutritional impact. Phosphoglycerate dehydrogenase is encoded by the PHGDH gene which is located on chromosome 1p12 and is composed of 17 exons that generate a protein of 533 amino acids.
Humans express two serine hydroxymethyltransferase genes, one is a soluble enzyme the other is located in the mitochondria.
The second reaction is a simple transamination catalyzed by phosphoserine aminotransferase 1 (PSAT1) which utilizes glutamate as the amino donor and releases 2-oxoglutarate (α-ketoglutarate). As for the catabolism of ornithine, the resulting Δ1-pyrroline-5-carboxylate is converted to glutamate via the action of ALDH4A1. Ornithine can be deaminated to Δ1-pyrroline-5-carboxylate via a reversal of the ornithine aminotransferase (OAT) reaction. This propionyl-CoA conversion pathway is also required for the metabolism of the amino acids valine, isoleucine, and methionine (see below), and odd-chain fatty acids. Methylmalony-CoA epimerase is encoded by the MCEE gene located on chromosome 2p13.3 and is composed of 4 exons that encode a 176 amino acid protein. The SUOX gene is located on chromosome 12q13.2 and is composed of 7 exons that encode a protein of 545 amino acids. The use of these alternative translational start sites generates mitochondrial and cytoplasmic or nuclear forms of the enzyme.
Cysteine catabolism and taurine synthesis both begin with the oxidation to cysteine sulfinic acid catalyzed by cysteine dioxygenase.
Synthesis of PAPS in humans is catalyzed by the bi-functional enzyme 3'-phosphoadenosine 5'-phosphosulfate synthase, PAPSS. For this reason this three-step reaction pathway is often remembered by the mnemonic as the VOMIT pathway, where V stands for valine, O for odd-chain fatty acids, M for methionine, I for isoleucine, and T for threonine. Methylmalonyl-CoA epimerase is encoded by the MCEE gene located on chromosome 2p13.3 and is composed of 4 exons that encode a 176 amino acid protein. The resulting α-ketoacids are then oxidatively decarboxylated via the action of the enzyme complex, branched-chain ketoacid dehydrogenase (BCKD). When your muscles are flooded with amino acids and in a blissful state of surplus, they use the excess to synthesize protein, which enhances recovery and ultimately helps build new muscle tissue.
We’re talking buckets on buckets, in the form of HQ dietary protein or supplementary BCAAs. But once those tanks are empty—depending on duration and intensity—it starts dipping into your amino acid pool. Sure you’ll lose weight, but if a large chunk of that is muscle, your body fat percentage might actually increase. In eukaryotes, there are only 21 proteinogenic amino acids, the 20 of the standard genetic code, plus selenocysteine. The mitochondrial AST enzyme is synthesized from the GOT2 gene that is located on chromosome 16q21 and is composed of 10 exons that generate two alternatively spliced mRNAs that encode two different isoforms: isoform 1 (430 amino acids) and isoform 2 (387 amino acids). Methionine synthase is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase) located on chromosome 1q43 and is composed of 34 exons that generate three alternatively spliced mRNAs.
The ALDH18A1 encoded enzyme is also known as delta-1-pyrroline-5-carboxylate synthase (P5CS). The reduction of Δ1-pyrroline-5-carboxylate to proline occurs via the action of pyrroline-5-carboxylate reductase 1 (PYCR1). The soluble enzyme is derived from the SHMT1 gene ocated on chromosome 17p11.2 which is composed of 13 exons that generate three alternatively spliced mRNAs. The resulting Δ1-pyrroline-5-carboxylate is oxidized to glutamate via the action of aldehyde dehydrogenase 4 family, member A1, ALDH4A1 (also called delta-1-pyrroline-5-carboxylate dehydrogenase, P5CDH). Methylmalonyl-CoA mutase is encoded by the MUT gene located on chromosome 6p12.3 and ius composed of 13 exons that encode a protein of 750 amino acids. The enzyme cysteine desulfurase (encoded by the NFS1 gene) is another important enzyme associated with cysteine catabolism. Cysteine sulfinate is converted to hypotaurine by the rate-limiting enzyme in taurine synthesis, cysteine sulfinic acid decarboxylase, CSAD (also called sulfinoalanine decarboxylase). Cysteine sulfinate is converted to taurine via the action of cysteinesulfinate decarboxylase. PAPSS possesses both the ATP sulfurylase and APS kinase activities that are associated with two separate enzymes in yeasts, bacteria, and plants.
Methylmalonyl-CoA mutase is encoded by the MUT gene located on chromosome 6p12.3 and is composed of 13 exons that encode a protein of 750 amino acids. The BCKD reaction generates the CoA derivatives of the decarboxylated ketoacids while also generating the reduced electron carrier, NADH. Humans can synthesize 12 of these from each other or from other molecules of intermediary metabolism. PRODH is proline dehydrogenase, the first enzyme in the pathway of proline catabolism which converts proline back to Δ1-pyrroline-5-carboxylate. The mitochondrial enzyme is derived from the SHMT2 gene located on chromosome 12q12–q14 which is composed of 14 exons that generate five altrernatively spliced mRNAs that encode three distinct isoforms of the enzyme. Catabolism of cysteine sulfinate to sulfate ion first involves a transamination that releases 3-sulfinpyruvate that spntaneously decomposes to bisulfite ion and pyruvate. After these first two reactions the remainder of the catabolic pathways for the three amino acids diverges. The other nine must be consumed (usually as their protein derivatives), and so they are called essential amino acids. Deficiency in either of these vitamins contributes to homocysteinemia and also to the development of macrocytic (megaloblastic) anemias. Ornithine aminotransferase utilizes glutamate as the amino donor and releases 2-oxoglutarate (α-ketoglutarate). In some tissues arginine serves as the precursor for nitric oxide (NO) production via the action of nitric oxide synthases (NOS). The sulfur remains associated with cysteine desulfurase and is subsequently transferred to numerous enzymes that possess iron-sulfur clusters for their activity. Oxidation of hypotaurine to taurine is thought to occur spontaneously, i.e non-enzymatically.
The transaminase responsible for this reaction is the soluble form of aspartate transaminase which is encoded by the GOT1 gene. 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. The essential amino acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine (i.e. The MAT1A gene is located on chromosome 10q22 and is composed of 10 exons that encode a protein of 395 amino acids. Cystathionine β-synthase is a PLP requiring enzyme demonstrating why B6 deficiency is also associated with the development of homocysteinemia. The ALDH18A1 gene is located on chromosome 10q24.3 and is composed of 18 exons that generate two alternatively spliced mRNAs encoding isoform 1 (795 amino acids) and isoform 2 (793 amino acids) versions of the enzyme.
The citrulline byproduct of the NOS reaction can feed back into arginine synthesis via the hepatic urea cycle enzymes argininosuccinate synthetase (ASS1) and argininosuccinate lyase (ASL).
The bisulfite ion is in ionic equilibrium with sulfite ion which is then converted to the sulfate ion via the action of sulfite oxidase. The MAT2A gene is located on chromosome 2p11.2 and is composed of 9 exons that encode a protein of 395 amino acids.
Mutations in the ALDH18A1 gene result is a disorder charaterized by hyperammonemia, hypoornithinemia, hypocitrullinemia, hypoargininemia and hypoprolinemia. Arginine also serves as the precursor for creatine synthesis and, therefore, arginine can be excreted in the urine as creatine byproduct, creatinine. The MAT2B gene is located on chromosome 5q34 and is composed of 8 exons that generate two alternatively spliced mRNAs encoding the MAT 2 beta isoform 1 (334 amino acids) and the MAT 2 beta isoform 2 (323 amino acids) enzymes.
This disorder is also associated with CNS degeneration, connective tissue disruption, and cataract formation. The cycling of citrulline back to arginine involves the urea cycle enzymes, argininosuccinate synthetase (ASS1) and argininosuccinate lyase (ASL). Ornithine aminotransferase is encoded by the OAT gene located on chromsome 10q26 and is composed of 12 exons that generate two alternatively spliced mRNAs.
The third reaction of leucine catabolism involves the enzyme isovaleryl-CoA dehydrogenase (IVD). The third reaction of valine catabolism involves the enzyme isobutyryl-CoA dehydrogenase (IBD).

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