Gene Association: ALDH4A1
UniProt Search:
ALDH4A1 (PROTEIN_CODING)
Function Description: aldehyde dehydrogenase 4 family member A1
found 21 associated metabolites with current gene based on the text mining result from the pubmed database.
Narcissin
Isorhamnetin-3-O-rutinoside is a disaccharide derivative, a glycosyloxyflavone, a monomethoxyflavone and a trihydroxyflavone. Narcissoside is a natural product found in Phoenix canariensis, Scolymus hispanicus, and other organisms with data available. See also: Ginkgo (part of); Calendula Officinalis Flower (part of). Acquisition and generation of the data is financially supported in part by CREST/JST. Narcissin (Narcissoside), a flavonol glycoside, exhibits evident scavenging activity against both authentic ONOO-?and SIN-1-derived ONOO- with IC50s?of 3.5 and 9.6 μM, respectively[1]. Narcissin (Narcissoside), a flavonol glycoside, exhibits evident scavenging activity against both authentic ONOO-?and SIN-1-derived ONOO- with IC50s?of 3.5 and 9.6 μM, respectively[1].
L-Proline
Proline (Pro), also known as L-proline is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. Proline is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Proline is found in all organisms ranging from bacteria to plants to animals. It is classified as an aliphatic, non-polar amino acid. Proline is sometimes called an imino acid, although the IUPAC definition of an imine requires a carbon-nitrogen double bond. Proline is a non-essential amino acid that is synthesized from glutamic acid. It is an essential component of collagen and is important for proper functioning of joints and tendons. Proline is derived from the amino acid L-glutamate in which glutamate-5-semialdehyde is first formed by glutamate 5-kinase and glutamate-5-semialdehyde dehydrogenase (which requires NADH or NADPH). This semialdehyde can then either spontaneously cyclize to form 1-pyrroline-5-carboxylic acid, which is reduced to proline by pyrroline-5-carboxylate reductase, or turned into ornithine by ornithine aminotransferase, followed by cyclization by ornithine cyclodeaminase to form proline. L-Proline has been found to act as a weak agonist of the glycine receptor and of both NMDA and non-NMDA ionotropic glutamate receptors. It has been proposed to be a potential endogenous excitotoxin/neurotoxin. Studies in rats have shown that when injected into the brain, proline non-selectively destroys pyramidal and granule cells (PMID: 3409032 ). Therefore, under certain conditions proline can act as a neurotoxin and a metabotoxin. A neurotoxin causes damage to nerve cells and nerve tissues. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of proline are associated with at least five inborn errors of metabolism, including hyperprolinemia type I, hyperprolinemia type II, iminoglycinuria, prolinemia type II, and pyruvate carboxylase deficiency. People with hyperprolinemia type I often do not show any symptoms even though they have proline levels in their blood between 3 and 10 times the normal level. Some individuals with hyperprolinemia type I exhibit seizures, intellectual disability, or other neurological or psychiatric problems. Hyperprolinemia type II results in proline levels in the blood between 10 and 15 times higher than normal, and high levels of a related compound called pyrroline-5-carboxylate. Hyperprolinemia type II has signs and symptoms that vary in severity and is more likely than type I to involve seizures or intellectual disability. L-proline is pyrrolidine in which the pro-S hydrogen at position 2 is substituted by a carboxylic acid group. L-Proline is the only one of the twenty DNA-encoded amino acids which has a secondary amino group alpha to the carboxyl group. It is an essential component of collagen and is important for proper functioning of joints and tendons. It also helps maintain and strengthen heart muscles. It has a role as a micronutrient, a nutraceutical, an algal metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a mouse metabolite and a member of compatible osmolytes. It is a glutamine family amino acid, a proteinogenic amino acid, a proline and a L-alpha-amino acid. It is a conjugate base of a L-prolinium. It is a conjugate acid of a L-prolinate. It is an enantiomer of a D-proline. It is a tautomer of a L-proline zwitterion. Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins. Proline is sometimes called an imino acid, although the IUPAC definition of an imine requires a carbon-nitrogen double bond. Proline is a non-essential amino acid that is synthesized from glutamic acid. It is an essential component of collagen and is important for proper functioning of joints and tendons. L-Proline is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Proline is a cyclic, nonessential amino acid (actually, an imino acid) in humans (synthesized from glutamic acid and other amino acids), Proline is a constituent of many proteins. Found in high concentrations in collagen, proline constitutes almost a third of the residues. Collagen is the main supportive protein of skin, tendons, bones, and connective tissue and promotes their health and healing. (NCI04) L-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins. Proline is sometimes called an imino acid, although the IUPAC definition of an imine requires a carbon-nitrogen double bond. Proline is a non-essential amino acid that is synthesized from glutamic acid. It is an essential component of collagen and is important for proper functioning of joints and tendons. A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons. Pyrrolidine in which the pro-S hydrogen at position 2 is substituted by a carboxylic acid group. L-Proline is the only one of the twenty DNA-encoded amino acids which has a secondary amino group alpha to the carboxyl group. It is an essential component of collagen and is important for proper functioning of joints and tendons. It also helps maintain and strengthen heart muscles. Flavouring ingredient; dietary supplement L-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins. L-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins.
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].
1-Pyrroline-5-carboxylic acid
1-Pyrroline-5-carboxylic acid (CAS: 2906-39-0) is an enamine or an imino acid that forms upon the spontaneous dehydration of L-glutamate gamma-semialdehyde in aqueous solutions. The stereoisomer (S)-1-pyrroline-5-carboxylate is an intermediate in glutamate metabolism, arginine degradation, and proline biosynthesis and degradation. It can also be converted into or be formed from three amino acids: L-glutamate, L-ornithine, and L-proline. In particular, it is synthesized via the oxidation of proline by pyrroline-5-carboxylate reductase 1 (PYCR1) (EC 1.5.1.2) or by proline dehydrogenase (PRODH) (EC 1.5.99.8). It is hydrolyzed into L-glutamate by delta-1-pyrroline-5-carboxylate dehydrogenase (ALDH4A1) (EC 1.5.1.12). It is also one of the few metabolites that can act as a precursor to other metabolites of both the urea cycle and the tricarboxylic acid (TCA) cycle. Under certain conditions, pyrroline-5-carboxylate can act as a neurotoxin and a metabotoxin. A neurotoxin causes damage to nerve cells and nerve tissues. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of pyrroline-5-carboxylate are associated with at least five inborn errors of metabolism, including hyperprolinemia type I, hyperprolinemia type II, iminoglycinuria, prolinemia type II, and pyruvate carboxylase deficiency. Hyperprolinemia type II results in high levels of pyrroline-5-carboxylate. People with hyperprolinemia type II have signs and symptoms that vary in severity, but they are more likely than type I to have seizures or intellectual disability. Pyrroline-5-carboxylate is highly reactive and excess quantities have been shown to cause cell death and apoptosis (PMID: 15548746). (s)-1-pyrroline-5-carboxylate, also known as delta-1-pyrroline-5-carboxylate, (+-)-isomer, belongs to alpha amino acids and derivatives class of compounds. Those are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon), or a derivative thereof (s)-1-pyrroline-5-carboxylate is soluble (in water) and a moderately acidic compound (based on its pKa). (s)-1-pyrroline-5-carboxylate can be found in a number of food items such as beech nut, mango, oyster mushroom, and other bread, which makes (s)-1-pyrroline-5-carboxylate a potential biomarker for the consumption of these food products (s)-1-pyrroline-5-carboxylate may be a unique E.coli metabolite.
Allysine
Allysine (CAS: 1962-83-0), also known as 2-amino-6-oxohexanoic acid or 6-oxonorleucine, belongs to the class of organic compounds known as alpha-amino acids. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Outside of the human body, allysine has been detected, but not quantified in, several different foods, such as winged beans, wasabi, common verbena, arrowhead, and oats. This could make allysine a potential biomarker for the consumption of these foods. Allysine is a derivative of lysine used in the production of elastin and collagen. It is produced by the actions of the enzyme lysyl oxidase in the extracellular matrix and is essential in the crosslink formation that stabilizes collagen and elastin.
Propanal
Propanal, also known as N-propionaldehyde or C2H5CHO, belongs to the class of organic compounds known as alpha-hydrogen aldehydes. These are aldehydes with the general formula HC(H)(R)C(=O)H, where R is an organyl group. Propanal exists in all living species, ranging from bacteria to humans. Propanal is an alcohol, cocoa, and earthy tasting compound. Outside of the human body, Propanal is found, on average, in the highest concentration within wild celeries and carrots. Propanal has also been detected, but not quantified in several different foods, such as purple lavers, black salsifies, strawberry guava, grapefruit/pummelo hybrids, and alaska wild rhubarbs. It is an aldehyde that consists of ethane bearing a formyl substituent. Isolated from various plant sources, e.g. hops, banana, sweet or sour cherry, blackcurrants, melon, pineapple, bread, chesses, coffee, cooked rice and strawberry or apple aroma. Flavouring agent
L-Glutamic gamma-semialdehyde
L-glutamic-gamma-semialdehyde, also known as 5-oxo-L-norvaline or glutamic acid gamma-semialdehyde, (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. L-glutamic-gamma-semialdehyde is soluble (in water) and a moderately acidic compound (based on its pKa). L-glutamic-gamma-semialdehyde can be found in a number of food items such as rubus (blackberry, raspberry), jackfruit, loganberry, and plains prickly pear, which makes L-glutamic-gamma-semialdehyde a potential biomarker for the consumption of these food products. L-glutamic-gamma-semialdehyde exists in all living species, ranging from bacteria to humans. In humans, L-glutamic-gamma-semialdehyde is involved in the arginine and proline metabolism. L-glutamic-gamma-semialdehyde is also involved in several metabolic disorders, some of which include hyperornithinemia-hyperammonemia-homocitrullinuria [hhh-syndrome], prolidase deficiency (PD), arginine: glycine amidinotransferase deficiency (AGAT deficiency), and ornithine aminotransferase deficiency (OAT deficiency). Glutamic gamma-semialdehyde is the metabolic precursor for proline biosynthesis. The conversion from L-Glutamate, an ATP- and NADPH-dependent reaction, is catalyzed by the enzyme Delta-1-pyrroline-5-carboxylate synthetase (P5CS) (OMIM 138250). L-Glutamic-gamma-semialdehyde can also be converted to or be formed from the amino acids L-ornithine (EC 2.6.1.13) and L-proline (EC 1.5.99.8 and EC 1.5.1.2). It is also one of the few metabolites that can be a precursor to other metabolites of both the urea cycle and the citric acid cycle (BioCyc).
1-Pyrroline-2-carboxylic acid
1-Pyrroline-2-carboxylic acid is a terminal product of D-proline metabolism. Specifically D-proline is converted to 1-Pyrroline-2-carboxylic acid via D-amino acid oxidase. This spontaneously breaks down to 2-oxo-5-amino-valerate. [HMDB] 1-Pyrroline-2-carboxylic acid is a terminal product of D-proline metabolism. Specifically D-proline is converted to 1-Pyrroline-2-carboxylic acid via D-amino acid oxidase. This spontaneously breaks down to 2-oxo-5-amino-valerate.
1-Pyrroline
Pyrrolines, also known under the name dihydropyrroles, are three different heterocyclic organic chemical compounds which differ in the position of the double bond. Pyrrolines are formally derived from the aromate pyrrole by hydrogenation. 1-Pyrroline is a cyclic imine while 2-pyrroline and 3-pyrroline are cyclic amines. Present in clam and squid. Flavouring agent for fish products and other foods. 3,4-Dihydro-2H-pyrrole is found in many foods, some of which are garden onion (variety), breadnut tree seed, chinese bayberry, and kiwi.
DL-Proline
Proline, also known as dl-proline or hpro, belongs to proline and derivatives class of compounds. Those are compounds containing proline or a derivative thereof resulting from reaction of proline at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. Proline is soluble (in water) and a moderately acidic compound (based on its pKa). Proline can be found in a number of food items such as yellow zucchini, swiss chard, spinach, and cucumber, which makes proline a potential biomarker for the consumption of these food products. Proline (abbreviated as Pro or P; encoded by the codons CCU, CCC, CCA, and CCG) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated NH2+ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain pyrrolidine, classifying it as a nonpolar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate . CONFIDENCE standard compound; ML_ID 53 (R)-pyrrolidine-2-carboxylic acid is an endogenous metabolite. (R)-pyrrolidine-2-carboxylic acid is an endogenous metabolite.
1-Pyrroline-5-carboxylic acid
A 1-pyrrolinecarboxylic acid that is 1-pyrroline in which one of the hydrogens at position 5 is replaced by a carboxy group. The stereoisomer (S)-1-pyrroline-5-carboxylate (also referred to as L-P5C) is an intermediate metabolite in the biosynthesis and degradation of proline and arginine.[4][5][6] In prokaryotic proline biosynthesis, GSA is synthesized from γ-glutamyl phosphate by the enzyme γ-glutamyl phosphate reductase. In most eukaryotes, GSA is synthesised from the amino acid glutamate by the bifunctional enzyme 1-pyrroline-5-carboxylate synthase (P5CS). The human P5CS is encoded by the ALDH18A1 gene.[7][8] The enzyme pyrroline-5-carboxylate reductase converts P5C into proline. In proline degradation, the enzyme proline dehydrogenase produces P5C from proline, and the enzyme 1-pyrroline-5-carboxylate dehydrogenase converts GSA to glutamate. In many prokaryotes, proline dehydrogenase and P5C dehydrogenase form a bifunctional enzyme that prevents the release of P5C during proline degradation. 1-Pyrroline-5-carboxylic acid. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=2906-39-0 (retrieved 2024-07-09) (CAS RN: 2906-39-0). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).
Proline
An alpha-amino acid that is pyrrolidine bearing a carboxy substituent at position 2. Acquisition and generation of the data is financially supported by the Max-Planck-Society L-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins. L-Proline is one of the twenty amino acids used in living organisms as the building blocks of proteins.
polyornithine
An optically active form of ornithine having L-configuration. 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].
1-Pyrroline-2-carboxylic acid
The product resulting from formal oxidation of DL-proline by loss of hydrogen from the nitrogen and from the carbon alpha to the carboxylic acid, with the formation of a C=N bond.
