Reaction Process: Plant Reactome:R-PTI-1119263
Arginine biosynthesis I related metabolites
find 18 related metabolites which is associated with chemical reaction(pathway) Arginine biosynthesis I
ATP + L-Asp + L-Cit ⟶ AMP + L-Argininosuccinate + PPi
Adenosine triphosphate
Adenosine triphosphate, also known as atp or atriphos, is a member of the class of compounds known as purine ribonucleoside triphosphates. Purine ribonucleoside triphosphates are purine ribobucleotides with a triphosphate group linked to the ribose moiety. Adenosine triphosphate is slightly soluble (in water) and an extremely strong acidic compound (based on its pKa). Adenosine triphosphate can be found in a number of food items such as lichee, alpine sweetvetch, pecan nut, and black mulberry, which makes adenosine triphosphate a potential biomarker for the consumption of these food products. Adenosine triphosphate can be found primarily in blood, cellular cytoplasm, cerebrospinal fluid (CSF), and saliva, as well as throughout most human tissues. Adenosine triphosphate exists in all living species, ranging from bacteria to humans. In humans, adenosine triphosphate is involved in several metabolic pathways, some of which include phosphatidylethanolamine biosynthesis PE(16:0/18:4(6Z,9Z,12Z,15Z)), carteolol action pathway, phosphatidylethanolamine biosynthesis PE(20:3(5Z,8Z,11Z)/15:0), and carfentanil action pathway. Adenosine triphosphate is also involved in several metabolic disorders, some of which include lysosomal acid lipase deficiency (wolman disease), phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1), propionic acidemia, and the oncogenic action of d-2-hydroxyglutarate in hydroxygluaricaciduria. Moreover, adenosine triphosphate is found to be associated with rachialgia, neuroinfection, stroke, and subarachnoid hemorrhage. Adenosine triphosphate is a non-carcinogenic (not listed by IARC) potentially toxic compound. Adenosine triphosphate is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalanc. Adenosine triphosphate (ATP) is a complex organic chemical that participates in many processes. Found in all forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts to either the di- or monophosphates, respectively ADP and AMP. Other processes regenerate ATP such that the human body recycles its own body weight equivalent in ATP each day. It is also a precursor to DNA and RNA . ATP is able to store and transport chemical energy within cells. ATP also plays an important role in the synthesis of nucleic acids. ATP can be produced by various cellular processes, most typically in mitochondria by oxidative phosphorylation under the catalytic influence of ATP synthase. The total quantity of ATP in the human body is about 0.1 mole. The energy used by human cells requires the hydrolysis of 200 to 300 moles of ATP daily. This means that each ATP molecule is recycled 2000 to 3000 times during a single day. ATP cannot be stored, hence its consumption must closely follow its synthesis (DrugBank). Metabolism of organophosphates occurs principally by oxidation, by hydrolysis via esterases and by reaction with glutathione. Demethylation and glucuronidation may also occur. Oxidation of organophosphorus pesticides may result in moderately toxic products. In general, phosphorothioates are not directly toxic but require oxidative metabolism to the proximal toxin. The glutathione transferase reactions produce products that are, in most cases, of low toxicity. Paraoxonase (PON1) is a key enzyme in the metabolism of organophosphates. PON1 can inactivate some organophosphates through hydrolysis. PON1 hydrolyzes the active metabolites in several organophosphates insecticides as well as, nerve agents such as soman, sarin, and VX. The presence of PON1 polymorphisms causes there to be different enzyme levels and catalytic efficiency of this esterase, which in turn suggests that different individuals may be more susceptible to the toxic effect of organophosphate exposure (T3DB). ATP is an adenosine 5-phosphate in which the 5-phosphate is a triphosphate group. It is involved in the transportation of chemical energy during metabolic pathways. It has a role as a nutraceutical, a micronutrient, a fundamental metabolite and a cofactor. It is an adenosine 5-phosphate and a purine ribonucleoside 5-triphosphate. It is a conjugate acid of an ATP(3-). An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. Adenosine triphosphate is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Adenosine-5-triphosphate is a natural product found in Chlamydomonas reinhardtii, Arabidopsis thaliana, and other organisms with data available. Adenosine Triphosphate is an adenine nucleotide comprised of three phosphate groups esterified to the sugar moiety, found in all living cells. Adenosine triphosphate is involved in energy production for metabolic processes and RNA synthesis. In addition, this substance acts as a neurotransmitter. In cancer studies, adenosine triphosphate is synthesized to examine its use to decrease weight loss and improve muscle strength. Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (A3367, A3368, A3369, A3370, A3371). Adenosine triphosphate is a metabolite found in or produced by Saccharomyces cerevisiae. An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (PMID: 15490415, 15129319, 14707763, 14696970, 11157473). 5′-ATP. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=56-65-5 (retrieved 2024-07-01) (CAS RN: 56-65-5). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).
Adenosine monophosphate
Adenosine monophosphate, also known as adenylic acid or amp, is a member of the class of compounds known as purine ribonucleoside monophosphates. Purine ribonucleoside monophosphates are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached. Adenosine monophosphate is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Adenosine monophosphate can be found in a number of food items such as kiwi, taro, alaska wild rhubarb, and skunk currant, which makes adenosine monophosphate a potential biomarker for the consumption of these food products. Adenosine monophosphate can be found primarily in most biofluids, including blood, feces, cerebrospinal fluid (CSF), and urine, as well as throughout all human tissues. Adenosine monophosphate exists in all living species, ranging from bacteria to humans. In humans, adenosine monophosphate is involved in several metabolic pathways, some of which include josamycin action pathway, methacycline action pathway, nevirapine action pathway, and aspartate metabolism. Adenosine monophosphate is also involved in several metabolic disorders, some of which include hyperornithinemia-hyperammonemia-homocitrullinuria [hhh-syndrome], molybdenum cofactor deficiency, xanthinuria type I, and mitochondrial DNA depletion syndrome. Adenosine monophosphate is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalanc. Adenosine monophosphate, also known as 5-adenylic acid and abbreviated AMP, is a nucleotide that is found in RNA. It is an ester of phosphoric acid with the nucleoside adenosine. AMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase adenine. AMP can be produced during ATP synthesis by the enzyme adenylate kinase. AMP has recently been approved as a Bitter Blocker additive to foodstuffs. When AMP is added to bitter foods or foods with a bitter aftertaste it makes them seem sweeter. This potentially makes lower calorie food products more palatable. [Spectral] AMP (exact mass = 347.06308) and Guanine (exact mass = 151.04941) and 3,4-Dihydroxy-L-phenylalanine (exact mass = 197.06881) and Glutathione disulfide (exact mass = 612.15196) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] AMP (exact mass = 347.06308) and Glutathione disulfide (exact mass = 612.15196) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] AMP (exact mass = 347.06308) and Adenine (exact mass = 135.0545) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Adenosine monophosphate. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=67583-85-1 (retrieved 2024-07-01) (CAS RN: 61-19-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Adenosine monophosphate is a key cellular metabolite regulating energy homeostasis and signal transduction. Adenosine monophosphate is a key cellular metabolite regulating energy homeostasis and signal transduction. Adenosine monophosphate is a key cellular metabolite regulating energy homeostasis and signal transduction.
Adenosine diphosphate
Adenosine diphosphate (ADP), also known as adenosine pyrophosphate (APP), is an important organic compound in metabolism and is essential to the flow of energy in living cells. ADP consists of three important structural components: a sugar backbone attached to adenine and two phosphate groups bonded to the 5 carbon atom of ribose. The diphosphate group of ADP is attached to the 5’ carbon of the sugar backbone, while the adenine attaches to the 1’ carbon. ADP belongs to the class of organic compounds known as purine ribonucleoside diphosphates. These are purine ribobucleotides with diphosphate group linked to the ribose moiety. It is an ester of pyrophosphoric acid with the nucleotide adenine. Adenosine diphosphate is a nucleotide. ADP exists in all living species, ranging from bacteria to humans. In humans, ADP is involved in d4-gdi signaling pathway. ADP is the product of ATP dephosphorylation by ATPases. ADP is converted back to ATP by ATP synthases. ADP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase adenine. Adenosine diphosphate, abbreviated ADP, is a nucleotide. It is an ester of pyrophosphoric acid with the nucleotide adenine. ADP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase adenine. 5′-ADP. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=58-64-0 (retrieved 2024-07-01) (CAS RN: 58-64-0). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Adenosine 5'-diphosphate (Adenosine diphosphate) is a nucleoside diphosphate. Adenosine 5'-diphosphate is the product of ATP dephosphorylation by ATPases. Adenosine 5'-diphosphate induces human platelet aggregation and inhibits stimulated adenylate cyclase by an action at P2T-purinoceptors. Adenosine 5'-diphosphate (Adenosine diphosphate) is a nucleoside diphosphate. Adenosine 5'-diphosphate is the product of ATP dephosphorylation by ATPases. Adenosine 5'-diphosphate induces human platelet aggregation and inhibits stimulated adenylate cyclase by an action at P2T-purinoceptors.
Oxoglutaric acid
Oxoglutaric acid, also known as alpha-ketoglutarate, alpha-ketoglutaric acid, AKG, or 2-oxoglutaric acid, is classified as a gamma-keto acid or a gamma-keto acid derivative. gamma-Keto acids are organic compounds containing an aldehyde substituted with a keto group on the C4 carbon atom. alpha-Ketoglutarate is considered to be soluble (in water) and acidic. alpha-Ketoglutarate is a key molecule in the TCA cycle, playing a fundamental role in determining the overall rate of this important metabolic process (PMID: 26759695). In the TCA cycle, AKG is decarboxylated to succinyl-CoA and carbon dioxide by AKG dehydrogenase, which functions as a key control point of the TCA cycle. Additionally, AKG can be generated from isocitrate by oxidative decarboxylation catalyzed by the enzyme known as isocitrate dehydrogenase (IDH). In addition to these routes of production, AKG can be produced from glutamate by oxidative deamination via glutamate dehydrogenase, and as a product of pyridoxal phosphate-dependent transamination reactions (mediated by branched-chain amino acid transaminases) in which glutamate is a common amino donor. AKG is a nitrogen scavenger and a source of glutamate and glutamine that stimulates protein synthesis and inhibits protein degradation in muscles. In particular, AKG can decrease protein catabolism and increase protein synthesis to enhance bone tissue formation in skeletal muscles (PMID: 26759695). Interestingly, enteric feeding of AKG supplements can significantly increase circulating plasma levels of hormones such as insulin, growth hormone, and insulin-like growth factor-1 (PMID: 26759695). It has recently been shown that AKG can extend the lifespan of adult C. elegans by inhibiting ATP synthase and TOR (PMID: 24828042). In combination with molecular oxygen, alpha-ketoglutarate is required for the hydroxylation of proline to hydroxyproline in the production of type I collagen. A recent study has shown that alpha-ketoglutarate promotes TH1 differentiation along with the depletion of glutamine thereby favouring Treg (regulatory T-cell) differentiation (PMID: 26420908). alpha-Ketoglutarate has been found to be associated with fumarase deficiency, 2-ketoglutarate dehydrogenase complex deficiency, and D-2-hydroxyglutaric aciduria, which are all inborn errors of metabolism (PMID: 8338207). Oxoglutaric acid has been found to be a metabolite produced by Corynebacterium and yeast (PMID: 27872963) (YMDB). [Spectral] 2-Oxoglutarate (exact mass = 146.02152) and S-Adenosyl-L-homocysteine (exact mass = 384.12159) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] 2-Oxoglutarate (exact mass = 146.02152) and (S)-Malate (exact mass = 134.02152) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Flavouring ingredient
Argininosuccinic acid disodium
C10H18N4O6 (290.12262880000003)
Arginosuccinic acid is a basic amino acid. Some cells synthesize it from citrulline, aspartic acid and use it as a precursor for arginine in the urea cycle or Citrulline-NO cycle. The enzyme that catalyzes the reaction is argininosuccinate synthetase. Argininosuccinic acid is a precursor to fumarate in the citric acid cycle via argininosuccinate lyase. Defects in the argininosuccinate lyase enzyme can lead to argininosuccinate lyase deficiency, which is an inborn error of metabolism. Argininosuccinate (ASA) lyase deficiency results in defective cleavage of ASA. This leads to an accumulation of ASA in cells and an excessive excretion of ASA in urine (argininosuccinic aciduria). In virtually all respects, this disorder shares the characteristics of other urea cycle defects. The most important characteristic of ASA lyase deficiency is its propensity to cause hyperammonemia in affected individuals. ASA in affected individuals is excreted by the kidney at a rate practically equivalent to the glomerular filtration rate (GFR). Whether ASA itself causes a degree of toxicity due to hepatocellular accumulation is unknown; such an effect could help explain hyperammonemia development in affected individuals. Regardless, the name of the disease is derived from the rapid clearance of ASA in urine, although elevated levels of ASA can be found in plasma. ASA lyase deficiency is associated with high mortality and morbidity rates. Symptoms of ASA lyase deficiency include anorexia, irritability rapid breathing, lethargy and vomiting. Extreme symptoms include coma and cerebral edema. Arginosuccinic acid is a basic amino acid. Some cells synthesize it from citrulline, aspartic acid and use it as a precursor for arginine in the urea cycle or Citrulline-NO cycle. The enzyme that catalyzes the reaction is argininosuccinate synthetase. Argininosuccinic acid is a precursor to fumarate in the citric acid cycle via argininosuccinate lyase. Defects in the arginosuccinate lyase enzyme can lead to arginosuccinate lyase deficiency. Argininosuccinate (ASA) lyase deficiency results in defective cleavage of ASA. This leads to an accumulation of ASA in cells and an excessive excretion of ASA in urine (arginosuccinic aciduria). In virtually all respects, this disorder shares the characteristics of other urea cycle defects. The most important characteristic of ASA lyase deficiency is its propensity to cause hyperammonemia in affected individuals. ASA in affected individuals is excreted by the kidney at a rate practically equivalent to the glomerular filtration rate (GFR). Whether ASA itself causes a degree of toxicity due to hepatocellular accumulation is unknown; such an effect could help explain hyperammonemia development in affected individuals. Regardless, the name of the disease is derived from the rapid clearance of ASA in urine, although elevated levels of ASA can be found in plasma. ASA lyase deficiency is associated with high mortality and morbidity rates. Symptoms of ASA lyase deficiency include anorexia, irritability rapid breathing, lethargy and vomiting. Extreme symptoms include coma and cerebral edema. [HMDB] KEIO_ID A039; [MS2] KO008844 KEIO_ID A039
N-acetylglutamate
N-Acetyl-L-glutamic acid or N-Acetylglutamate, belongs to the class of organic compounds known as N-acyl-alpha amino acids. N-acyl-alpha amino acids are compounds containing an alpha amino acid which bears an acyl group at its terminal nitrogen atom. N-Acetyl-L-glutamate can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetyl-L-glutamate is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-glutamic acid. N-Acetyl-L-glutamic acid is found in all organisms ranging from bacteria to plants to animals. N-acetyl amino acids can be produced either via direct synthesis of specific N-acetyltransferases or via the proteolytic degradation of N-acetylated proteins by specific hydrolases. N-terminal acetylation of proteins is a widespread and highly conserved process in eukaryotes that is involved in protection and stability of proteins (PMID: 16465618). About 85\\\\% of all human proteins and 68\\\\% of all yeast proteins are acetylated at their N-terminus (PMID: 21750686). Several proteins from prokaryotes and archaea are also modified by N-terminal acetylation. The majority of eukaryotic N-terminal-acetylation reactions occur through N-acetyltransferase enzymes or NAT’s (PMID: 30054468). These enzymes consist of three main oligomeric complexes NatA, NatB, and NatC, which are composed of at least a unique catalytic subunit and one unique ribosomal anchor. The substrate specificities of different NAT enzymes are mainly determined by the identities of the first two N-terminal residues of the target protein. The human NatA complex co-translationally acetylates N-termini that bear a small amino acid (A, S, T, C, and occasionally V and G) (PMID: 30054468). NatA also exists in a monomeric state and can post-translationally acetylate acidic N-termini residues (D-, E-). NatB and NatC acetylate N-terminal methionine with further specificity determined by the identity of the second amino acid. N-acetylated amino acids, such as N-acetylglutamate can be released by an N-acylpeptide hydrolase from peptides generated by proteolytic degradation (PMID: 16465618). In addition to the NAT enzymes and protein-based acetylation, N-acetylation of free glutamic acid can also occur. In particular, N-Acetyl-L-glutamic acid can be biosynthesized from glutamate and acetylornithine by ornithine acetyltransferase, and from glutamic acid and acetyl-CoA by the enzyme known as N-acetylglutamate synthase. N-Acetyl-L-glutamic acid is the first intermediate involved in the biosynthesis of arginine in prokaryotes and simple eukaryotes and a regulator of the urea cycle in vertebrates. In vertebrates, N-acetylglutamic acid is the allosteric activator molecule to mitochondrial carbamyl phosphate synthetase I (CPSI) which is the first enzyme in the urea cycle. It triggers the production of the first urea cycle intermediate, a compound known as carbamyl phosphate. Notably the CPSI enzyme is inactive when N-acetylglutamic acid is not present. A deficiency in N-acetyl glutamate synthase or a genetic mutation in the gene coding for the enzyme will lead to urea cycle failure in which ammonia is not converted to urea, but rather accumulated in the blood leading to the condition called Type I hyperammonemia. Excessive amounts N-acetyl amino acids can be detected in the urine with individuals with aminoacylase I deficiency, a genetic disorder (PMID: 16465618). These include N-acetylalanine (as well as N-acetylserine, N-acetylglutamine, N-acetylglutamate, N-acetylglycine, N-acetylmethionine and smaller amounts of N-acetylthreonine, N-acetylleucine, N-acetylvaline and N-acetylisoleucine. Aminoacylase I is a soluble homodimeric zinc binding enzyme that catalyzes the formation of free aliphatic amino acids from N-acetylated precursors. In humans, Aminoacylase I is encoded by the aminoacylase 1 gene (ACY1) on chromosome 3p21 that consists of 15 exons (OMIM 609924). Individuals with aminoacylase I deficiency w... N-acetyl-l-glutamate, also known as L-N-acetylglutamic acid or ac-glu-oh, belongs to glutamic acid and derivatives class of compounds. Those are compounds containing glutamic acid or a derivative thereof resulting from reaction of glutamic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. N-acetyl-l-glutamate is soluble (in water) and a weakly acidic compound (based on its pKa). N-acetyl-l-glutamate can be found in a number of food items such as cardoon, almond, butternut squash, and avocado, which makes N-acetyl-l-glutamate a potential biomarker for the consumption of these food products. N-acetyl-l-glutamate may be a unique S.cerevisiae (yeast) metabolite. Acquisition and generation of the data is financially supported in part by CREST/JST. KEIO_ID A031 N-Acetyl-L-glutamic acid, a glutamic acid, is a component of animal cell culturing media. N-Acetyl-L-glutamic acid is a metabolite of Saccharomyces cerevisiae and human[1]. N-Acetyl-L-glutamic acid, a glutamic acid, is a component of animal cell culturing media. N-Acetyl-L-glutamic acid is a metabolite of Saccharomyces cerevisiae and human[1].
N-alpha-acetylornithine
N2-Acetylornithine, also known as N(alpha)-acetylornithine, belongs to the class of organic compounds known as N-acyl-L-alpha-amino acids. These are N-acylated alpha-amino acids which have the L-configuration of the alpha-carbon atom. N-Acetylornithine is a minor component of the deproteinized blood plasma of human blood. Human blood plasma contains a variable amount of acetylornithine, averaging 1.1 +/- 0.4 umol/L (range 0.8-0.2 umol/L). Urine contains a very small amount of acetylornithine, approximately 1 nmol/mg creatinine (1 umol/day) (PMID:508804). Acquisition and generation of the data is financially supported in part by CREST/JST. CONFIDENCE standard compound; INTERNAL_ID 160 KEIO_ID A032 N-Acetylornithine is an intermediate in the enzymatic biosynthesis of the amino acid L-arginine from L-glutamate.
L-Ornithine
Ornithine, also known as (S)-2,5-diaminopentanoic acid or ornithine, (L)-isomer, is a member of the class of compounds known as L-alpha-amino acids. L-alpha-amino acids are alpha amino acids which have the L-configuration of the alpha-carbon atom. Ornithine is soluble (in water) and a moderately acidic compound (based on its pKa). Ornithine can be found in a number of food items such as pine nut, lingonberry, turnip, and cassava, which makes ornithine a potential biomarker for the consumption of these food products. Ornithine can be found primarily in most biofluids, including urine, cerebrospinal fluid (CSF), feces, and saliva, as well as throughout most human tissues. Ornithine exists in all living species, ranging from bacteria to humans. In humans, ornithine is involved in few metabolic pathways, which include arginine and proline metabolism, glycine and serine metabolism, spermidine and spermine biosynthesis, and urea cycle. Ornithine is also involved in several metabolic disorders, some of which include ornithine transcarbamylase deficiency (OTC deficiency), prolidase deficiency (PD), citrullinemia type I, and arginine: glycine amidinotransferase deficiency (AGAT deficiency). Moreover, ornithine is found to be associated with cystinuria, alzheimers disease, leukemia, and uremia. Ornithine is a non-carcinogenic (not listed by IARC) potentially toxic compound. Ornithine is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalance. it has been claimed that ornithine improves athletic performance, has anabolic effects, has wound-healing effects, and is immuno-enhancing. Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl . L-Ornithine is metabolised to L-arginine. L-arginine stimulates the pituitary release of growth hormone. Burns or other injuries affect the state of L-arginine in tissues throughout the body. As De novo synthesis of L-arginine during these conditions is usually not sufficient for normal immune function, nor for normal protein synthesis, L-ornithine may have immunomodulatory and wound-healing activities under these conditions (by virtue of its metabolism to L-arginine) (DrugBank). Chronically high levels of ornithine are associated with at least 9 inborn errors of metabolism including: Cystathionine Beta-Synthase Deficiency, Hyperornithinemia with gyrate atrophy, Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, Hyperprolinemia Type II, Lysinuric Protein Intolerance, Ornithine Aminotransferase Deficiency, Ornithine Transcarbamylase Deficiency and Prolinemia Type II (T3DB). Ornithine or L-ornithine, also known as (S)-2,5-diaminopentanoic acid is a member of the class of compounds known as L-alpha-amino acids. L-alpha-amino acids are alpha amino acids which have the L-configuration of the alpha-carbon atom. L-ornithine is soluble (in water) and a moderately basic compound. Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. It is considered to be a non-essential amino acid. A non-essential amino acid is an amino acid that can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Outside the human body, L-ornithine is abundant in a number of food items such as wild rice, brazil nuts, common oregano, and common grapes. L-ornithine can be found throughout most human tissues; and in most biofluids, some of which include blood, urine, cerebrospinal fluid (CSF), sweat, saliva, and feces. L-ornithine exists in all living species, from bacteria to plants to humans. L-Ornithine is also a precursor of citrulline and arginine. In order for ornithine that is produced in the cytosol to be converted to citrulline, it must first cross the inner mitochondrial membrane into the mitochondrial matrix where it is carbamylated by the enzyme known as ornithine transcarbamylase. This transfer is mediated by the mitochondrial ornithine transporter (SLC25A15; AF112968; ORNT1). Mutations in the mitochondrial ornithine transporter result in hyperammonemia, hyperornithinemia, homocitrullinuria (HHH) syndrome, a disorder of the urea cycle (PMID: 16256388). The pathophysiology of the disease may involve diminished ornithine transport into mitochondria, resulting in ornithine accumulation in the cytoplasm and reduced ability to clear carbamoyl phosphate and ammonia loads (OMIM 838970). In humans, L-ornithine is involved in a number of other metabolic disorders, some of which include, ornithine transcarbamylase deficiency (OTC deficiency), argininemia, and guanidinoacetate methyltransferase deficiency (GAMT deficiency). Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. Moreover, Ornithine is found to be associated with cystinuria, hyperdibasic aminoaciduria I, and lysinuric protein intolerance, which are inborn errors of metabolism. It has been claimed that ornithine improves athletic performance, has anabolic effects, has wound-healing effects, and is immuno-enhancing. L-Ornithine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=70-26-8 (retrieved 2024-07-01) (CAS RN: 70-26-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Ornithine ((S)-2,5-Diaminopentanoic acid) is a non-proteinogenic amino acid, is mainly used in urea cycle removing excess nitrogen in vivo. L-Ornithine shows nephroprotective[1][2]. L-Ornithine ((S)-2,5-Diaminopentanoic acid) is a non-proteinogenic amino acid, is mainly used in urea cycle removing excess nitrogen in vivo. L-Ornithine shows nephroprotective[1][2].
Nicotinamide adenine dinucleotide phosphate
NADPH is the reduced form of NADP+, and NADP+ is the oxidized form of NADPH. Nicotinamide adenine dinucleotide phosphate (NADP) is a coenzyme composed of ribosylnicotinamide 5-phosphate (NMN) coupled with a pyrophosphate linkage to 5-phosphate adenosine 2,5-bisphosphate. NADP serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). NADP is formed through the addition of a phosphate group to the 2 position of the adenosyl nucleotide through an ester linkage (Dorland, 27th ed). This extra phosphate is added by the enzyme NAD+ kinase and removed via NADP+ phosphatase. NADP is also known as TPN (triphosphopyridine nucleotide) and it is an important cofactor used in anabolic reactions in all forms of cellular life. Examples include the Calvin cycle, cholesterol synthesis, fatty acid elongation, and nucleic acid synthesis (Wikipedia). Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5-phosphate (NMN) coupled by pyrophosphate linkage to the 5-phosphate adenosine 2,5-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed.) [HMDB]. NADPH is found in many foods, some of which are american pokeweed, rice, ginseng, and ostrich fern. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS
Citrulline
Citrulline, also known as Cit or δ-ureidonorvaline, belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom. Citrulline has the formula H2NC(O)NH(CH2)3CH(NH2)CO2H. Citrulline exists in all living species, ranging from bacteria to humans. Within humans, citrulline participates in a number of enzymatic reactions. In particular, citrulline can be biosynthesized from carbamoyl phosphate and ornithine which is catalyzed by the enzyme ornithine carbamoyltransferase. In addition, citrulline and L-aspartic acid can be converted into argininosuccinic acid through the action of the enzyme argininosuccinate synthase. In humans, citrulline is involved in the metabolic disorder called argininemia. Citrulline has also been found to be associated with several diseases such as ulcerative colitis, rheumatoid arthritis, and citrullinemia type II. Citrulline has also been linked to several inborn metabolic disorders including argininosuccinic aciduria and fumarase deficiency. Outside of the human body, citrulline is found, on average, in the highest concentration in a few different foods such as wheats, oats, and cucumbers and in a lower concentration in swiss chards, yellow wax beans, and potato. Citrulline has also been detected, but not quantified in several different foods, such as epazotes, lotus, common buckwheats, strawberry guava, and italian sweet red peppers. Citrulline is a potentially toxic compound. Proteins that normally contain citrulline residues include myelin basic protein (MBP), filaggrin, and several histone proteins, whereas other proteins, such as fibrin and vimentin are susceptible to citrullination during cell death and tissue inflammation. Citrulline is also produced as a byproduct of the enzymatic production of nitric oxide from the amino acid arginine, catalyzed by nitric oxide synthase. It is also produced from arginine as a byproduct of the reaction catalyzed by NOS family (NOS; EC1.14.13.39). [Spectral] L-Citrulline (exact mass = 175.09569) and L-Glutamate (exact mass = 147.05316) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Acquisition and generation of the data is financially supported in part by CREST/JST. COVID info from clinicaltrial, clinicaltrials, clinical trial, clinical trials Occurs in the juice of watermelon (Citrullus vulgaris) IPB_RECORD: 257; CONFIDENCE confident structure KEIO_ID C013 Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS 2-Amino-5-ureidopentanoic acid is an endogenous metabolite. 2-Amino-5-ureidopentanoic acid is an endogenous metabolite. L-Citrulline is an amino acid derived from ornithine in the catabolism of proline or glutamine and glutamate, or from l-arginine via arginine-citrulline pathway. L-Citrulline is an amino acid derived from ornithine in the catabolism of proline or glutamine and glutamate, or from l-arginine via arginine-citrulline pathway.
NADP+
[C21H29N7O17P3]+ (744.0832754)
[Spectral] NADP+ (exact mass = 743.07545) and NAD+ (exact mass = 663.10912) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS
Pyrophosphate
The anion, the salts, and the esters of pyrophosphoric acid are called pyrophosphates. The pyrophosphate anion is abbreviated PPi and is formed by the hydrolysis of ATP into AMP in cells. This hydrolysis is called pyrophosphorolysis. The pyrophosphate anion has the structure P2O74-, and is an acid anhydride of phosphate. It is unstable in aqueous solution and rapidly hydrolyzes into inorganic phosphate. Pyrophosphate is an osteotoxin (arrests bone development) and an arthritogen (promotes arthritis). It is also a metabotoxin (an endogenously produced metabolite that causes adverse health affects at chronically high levels). Chronically high levels of pyrophosphate are associated with hypophosphatasia. Hypophosphatasia (also called deficiency of alkaline phosphatase or phosphoethanolaminuria) is a rare, and sometimes fatal, metabolic bone disease. Hypophosphatasia is associated with a molecular defect in the gene encoding tissue non-specific alkaline phosphatase (TNSALP). TNSALP is an enzyme that is tethered to the outer surface of osteoblasts and chondrocytes. TNSALP hydrolyzes several substances, including inorganic pyrophosphate (PPi) and pyridoxal 5-phosphate (PLP), a major form of vitamin B6. When TSNALP is low, inorganic pyrophosphate (PPi) accumulates outside of cells and inhibits the formation of hydroxyapatite, one of the main components of bone, causing rickets in infants and children and osteomalacia (soft bones) in adults. Vitamin B6 must be dephosphorylated by TNSALP before it can cross the cell membrane. Vitamin B6 deficiency in the brain impairs synthesis of neurotransmitters which can cause seizures. In some cases, a build-up of calcium pyrophosphate dihydrate crystals in the joints can cause pseudogout. COVID info from WikiPathways Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS
Carbamoyl phosphate
Carbamoyl phosphate is a precursor of both arginine and pyrimidine biosynthesis. It is a labile and potentially toxic intermediate. Carbamoyl phosphate is a molecule that is involved in ridding the body of excess nitrogen in the urea cycle, and also in the synthesis of pyrimidines. It is produced from carbon dioxide, ammonia, and phosphate (from ATP) by the enzyme carbamoyl phosphate synthase. -- Wikipedia. Carbamoyl phosphate is a molecule that is involved in ridding the body of excess nitrogen in the urea cycle, and also in the synthesis of pyrimidines. It is produced from carbon dioxide, ammonia, and phosphate (from ATP) by the enzyme carbamoyl phosphate synthase. -- Wikipedia [HMDB]. Carbamoylphosphate is found in many foods, some of which are pepper (spice), rapini, endive, and rye.
N-Acetyl-L-glutamate 5-semialdehyde
N-Acetyl-L-glutamate 5-semialdehyde is an intermediate in Urea cycle and metabolism of amino groups. N-Acetyl-L-glutamate 5-semialdehyde is the. second to last step in the synthesis of L-Ornithine and is converted. from N-Acetyl-L-glutamate 5-phosphate via the enzyme N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38). It is then converted to N-Acetylornithine via the enzyme acetylornithine aminotransferase (EC 2.6.1.11). N-Acetyl-L-glutamate 5-semialdehyde is an intermediate in Urea cycle and metabolism of amino groups. N-Acetyl-L-glutamate 5-semialdehyde is the
N-Acetyl-L-glutamyl 5-phosphate
N-Acetyl-L-glutamyl 5-phosphate is an intermediate in urea cycle and metabolism of amino groups. The enzyme N-acetyl-gamma-glutamyl-phosphate reductase [EC:1.2.1.38] catalyzes the conversion of this metabolite into N-acetyl-L-glutamate 5-semialdehyde. This reaction is irreversible and occurs in the mitochondria. (BiGG database) [HMDB] N-Acetyl-L-glutamyl 5-phosphate is an intermediate in urea cycle and metabolism of amino groups. The enzyme N-acetyl-gamma-glutamyl-phosphate reductase [EC:1.2.1.38] catalyzes the conversion of this metabolite into N-acetyl-L-glutamate 5-semialdehyde. This reaction is irreversible and occurs in the mitochondria. (BiGG database).
(2S)-2-ammoniobutanedioate
D018377 - Neurotransmitter Agents > D018846 - Excitatory Amino Acids
L-glutamate(1-)
An alpha-amino-acid anion that is the conjugate base of L-glutamic acid, having anionic carboxy groups and a cationic amino group
