Classification Term: 2154
N-acyl-L-alpha-amino acids (ontology term: CHEMONTID:0004148)
N-acylated alpha amino acids which have the L-configuration of the alpha-carbon atom." []
found 24 associated metabolites at no_class-level_9 metabolite taxonomy ontology rank level.
Ancestor: N-acyl-alpha amino acids
Child Taxonomies: N-acyl-L-glutamines
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.
N-Acetyltryptophan
N-Acetyl-L-tryptophan or N-Acetyltryptophan, 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-Acetyltryptophan can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetyltryptophan is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-tryptophan. 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-acetyltryptophan 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 tryptophan can also occur. Many N-acetylamino acids, including N-acetyltryptophan are classified as uremic toxins if present in high abundance in the serum or plasma (PMID: 26317986; PMID: 20613759). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). N-Acetyltryptophan has also been used as a protein stabilizer. It prevents protein molecules from oxidative degradation by scavenging oxygen dissolved in protein solutions (PMID: 21903216 ). N-Acetyltryptophan has been identified as a catabolite of tryptophan generated by the gut microbiota. After absorption through the intestinal epithelium, tryptophan catabolites enter the bloodstream and are later excreted in the urine (PMID: 28916042). N-Acetyltryptophan is an inhibitor of cytochrome c release and an antagonist of the neurokinin 1 receptor (NK-1R). These inhibitory effects are thought have a useful role in neuroprotection. For instance, in mouse models of amyotrophic lateral sclerosis (ALS) the administration of N-Acetyltryptophan has been shown delay disease onset, extend survival, and ameliorate deterioration in motor performance ALS transgenic mice (PMID: 25986728). N-acetyltryptophan has been shown to significantly reduce blood-brain barrier permeability and improve functional outcome in rat models of traumatic brain injury (PMID: 29256408). N-Acetyltryptophan has also been shown to have a role in preventing hepatic ischemia-reperfusion injury. This is thought to occur through de-activation of the RIP2/caspase/IL-1beta signaling pathway (PMID: 31184936). D004791 - Enzyme Inhibitors > D011480 - Protease Inhibitors Ac-DL-Trp-OH is an endogenous metabolite. Ac-DL-Trp-OH is an endogenous metabolite. N-Acetyl-L-tryptophan is an endogenous metabolite.
N-acetylcitrulline
N-alpha-Acetyl-L-citrulline, also known as N-acetylcitrulline, is an N-acetylated metabolite of citrulline that is part of the arginine biosynthetic pathway. Arginine biosynthesis is notable for its complexity and variability at the genetic level, and by its connection with several other pathways, such as pyrimidine and polyamine biosynthesis, and certain degradative pathways. The initial steps of the arginine biosynthetic pathways proceed via N-acetylated intermediates. The presumed reason for this is that the acetylation prevents the spontaneous cyclization of glutamate derivatives, which leads to proline biosynthesis. N-acetyl-L-ornithine can be transcarbamylated directly by the enzyme acetylornithine transcarbamylase, resulting in N-acetyl-L-citrulline. The enzyme acetylornithine deacetylase can accept N-acetyl-L-citrulline as a substrate and can deacetylate it into citrulline. N-alpha-Acetyl-L-citrulline is found in cases of deficiency of the urea cycle enzyme argininosuccinate synthase (EC 6.3.4.5) that leads to increased concentrations of citrulline and N-acetylcitrulline in the urine (PMID: 14633929). N-acetyl-l-citrulline, also known as (S)-2-acetamido-5-ureidopentanoic acid, is a member of the class of compounds known as N-acyl-l-alpha-amino acids. N-acyl-l-alpha-amino acids are n-acylated alpha amino acids which have the L-configuration of the alpha-carbon atom. N-acetyl-l-citrulline is slightly soluble (in water) and a weakly acidic compound (based on its pKa). N-acetyl-l-citrulline can be found in a number of food items such as macadamia nut, persian lime, broccoli, and annual wild rice, which makes N-acetyl-l-citrulline a potential biomarker for the consumption of these food products.
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-Succinyl-L,L-2,6-diaminopimelate
N-Succinyl-L,L-2,6-diaminopimelate is an intermediate in lysine biosynthesis. It is the third to last step in the synthesis of lysine and is converted. from N-Succinyl-2-amino-6-ketopimelate via the enzyme succinyldiaminopimelate transferase (EC 2.6.1.17). It is then converted to L,L-diaminopimelate via the enzyme succinyl-diaminopimelate desuccinylase (EC 3.5.1.18). N-Succinyl-L,L-2,6-diaminopimelate is an intermediate in lysine biosynthesis. It is the third to last step in the synthesis of lysine and is converted
N-Succinyl-2-amino-6-ketopimelate
N-Succinyl-2-amino-6-ketopimelate is an intermediate in lysine biosynthesis. It is the fourth to last step in the synthesis of lysine and is converted. from tetrahydrodipicolinate via the enzyme tetrahydrodipicolinate N-succinyltransferase (EC 2.3.1.117). It is then converted to N-succinyl-L,L-2,6-diaminopimelate via the enzyme Succinyldiaminopimelate transferase (EC 2.6.1.17). N-Succinyl-2-amino-6-ketopimelate is an intermediate in lysine biosynthesis. It is the fourth to last step in the synthesis of lysine and is converted
N2-Succinyl-L-glutamic acid 5-semialdehyde
N2-Succinyl-L-glutamic acid 5-semialdehyde is a substrate for Succinate semialdehyde dehydrogenase (mitochondrial) and Ornithine aminotransferase (mitochondrial). It can be found in Escherichia (UniProt). N2-Succinyl-L-glutamic acid 5-semialdehyde is a substrate for Succinate semialdehyde dehydrogenase (mitochondrial) and Ornithine aminotransferase (mitochondrial). [HMDB]
N-Acetylserine
N-Acetyl-L-serine or N-Acetylserine, 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-Acetylserine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetylserine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-serine. 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-acetylserine 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 serine can also occur. Excessive amounts N-acetyl amino acids including N-acetylserine (as well as N-acetylglycine, N-acetylglutamine, N-acetylmethionine, N-acetylglutamate, N-acetylalanine, N-acetylleucine and smaller amounts of N-acetylthreonine, N-acetylisoleucine, and N-acetylvaline) can be detected in the urine with individuals with acylase I deficiency, a genetic disorder (PMID: 16465618). 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 will experience convulsions, hearing loss and difficulty feeding (PMID: 16465618). ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. Many N-acetylamino acids, including N-acetylserine are classified as uremic toxins if present in high abundance in the serum or plasma (PMID: 26317986; PMID: 20613759). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). Acetylation of the N-terminal amino acid (-NH2 acetylation) is a common protein modification in eukaryotes but is rarely encountered in prokaryotes. In mammalians,80 to 90 percent of the cytosolic proteins are subjected to an irreversible, cotranslational amino acid acetylation at their N-terminus. Acetylation of the N-terminal amino acid (-NH2 acetylation) is a common protein modification in eukaryotes but is rarely encountered in prokaryotes. In mammalians, 80 to 90 percent of the cytosolic proteins are subjected to an irreversible, cotranslational amino acid acetylation at their N-terminus. N-acetylated proteins are catabolized in the cytosol by the ATP-ubiquitin-dependent proteasomal pathway. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase I (ACY1; EC 3.5.1.14), the most abundant type, is a soluble homodimeric zinc binding enzyme that catalyzes the formation of free aliphatic amino acids from N-acetylated precursors. It is encoded by the aminoacylase 1 gene (ACY1) on chromosome 3p21 that comprises 15 exons (OMIM 609924). Preferred substrates of ACY1 are aliphatic amino acids with a short-chain acyl moiety, especially N-acetyl-methionine. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. Functional aminoacylase I is crucial in the last step in this degradation as it catalyzes the hydrolysis of N-acetylated amino acids into acetate and the free amino acid. Although N-acetylation occurs in many metabolic pathways and N-acetylated metabolites are known to accumulate in several inborn errors, there are only a few reports on N-acetylated amino acids detected in urine. Identification of N-acetylated amino acids by routine GC-MS may be problematic for several reasons. The major problem is linked to the identification strategy itself. Identification of an unknown compound in mass spectrometry is usually based on comparison of its spectrum against a library of reference spectra. (PMID: 16465618, 16274666, 17723438). N-Acetyl-L-serine is found in watermelon.
Acetylcysteine
N-Acetyl-L-cysteine (NAC) or N-Acetylcysteine is the N-acetyl derivative of the amino acid L-cysteine and is a precursor in the formation of the antioxidant glutathione in the body. N-Acetylcysteine, 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-cysteine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetyl-L-cysteine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-cysteine. 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-acetylcysteine 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 cysteine can also occur. The enzyme known as cysteine-S-conjugate N-acetyltransferase (EC 2.3.1.80) catalyzes the transfer of the acetyl group of acetyl CoA to the amino group of cysteine. This enzyme is an important participant in glutathione metabolism and the production of glutathione. The thiol (sulfhydryl) group in N-Acetylcysteine confers antioxidant effects and is able to reduce free radicals. N-Acetylcysteine is a pharmacological agent used in the management of paracetamol (acetaminophen) overdoses. When acetaminophen is taken in large quantities, a minor metabolite called N-acetyl-p-benzoquinone imine (NAPQI) accumulates within the body. NAPQI is normally conjugated by glutathione, but when taken in excess, the bodys glutathione reserves are not sufficient to deactivate the toxic NAPQI. In the treatment of acetaminophen overdose, N-acetylcysteine acts to maintain or replenish depleted glutathione reserves in the liver and enhance non-toxic metabolism of acetaminophen. These actions serve to protect liver cells from NAPQI toxicity. For this particular indication, N-acetylcysteine is available under the trade names Mucomyst (Bristol-Myers Squibb) and Parvolex (GSK). N-Acetylcysteine is also used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates. Acetylcysteine has been studied for a number of psychiatric disorders. There is tentative evidence for N-acetylcysteine being useful in the treatment of Alzheimers disease, autism, bipolar disorder, drug-induced neuropathy, major depressive disorder, obsessive-compulsive disord... R - Respiratory system > R05 - Cough and cold preparations > R05C - Expectorants, excl. combinations with cough suppressants > R05CB - Mucolytics V - Various > V03 - All other therapeutic products > V03A - All other therapeutic products > V03AB - Antidotes COVID info from clinicaltrial, clinicaltrials, clinical trial, clinical trials C78273 - Agent Affecting Respiratory System > C74536 - Mucolytic Agent D019141 - Respiratory System Agents > D005100 - Expectorants D000890 - Anti-Infective Agents > D000998 - Antiviral Agents D000975 - Antioxidants > D016166 - Free Radical Scavengers Effective inhibitor of enzymic browning in foods [DFC] D020011 - Protective Agents > D000975 - Antioxidants C26170 - Protective Agent > C275 - Antioxidant S - Sensory organs > S01 - Ophthalmologicals Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS Acetylcysteine (N-Acetylcysteine) is a mucolytic agent which reduces the thickness of the mucus. Acetylcysteine is a ROS inhibitor[1]. Acetylcysteine is a cysteine precursor, prevents hemin-induced ferroptosis by neutralizing toxic lipids generated by arachidonate-dependent activity of 5-lipoxygenases[5]. Acetylcysteine induces cell apoptosis[2][3]. Acetylcysteine also has anti-influenza virus activities[7]. Acetylcysteine (N-Acetylcysteine) is a mucolytic agent which reduces the thickness of the mucus. Acetylcysteine is a ROS inhibitor[1]. Acetylcysteine is a cysteine precursor, prevents hemin-induced ferroptosis by neutralizing toxic lipids generated by arachidonate-dependent activity of 5-lipoxygenases[5]. Acetylcysteine induces cell apoptosis[2][3]. Acetylcysteine also has anti-influenza virus activities[7].
N-acetylalanine
N-Acetyl-L-alanine or N-Acetylalanine, 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-alanine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-alpha-Acetyl-L-alanine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-alanine. 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-Acetyl-L-alanine is a product of the enzyme known as ribosomal alanine N-acetyltransferase (EC 2.3.1.128) which catalyzes the transfer of the acetyl group of acetyl CoA to proteins bearing an N-terminal alanine. N-acetylated amino acids, such as N-acetylalanine can be released by an N-acylpeptide hydrolase from peptides generated by proteolytic degradation (PMID: 16465618). 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 will experience convulsions, hearing loss and difficulty feeding (PMID: 16465618). ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. Many N-acetylamino acids, including N-acetylalanine, are classified as uremic toxins (PMID: 26317986; PMID: 20613759). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). N-Acetyl-L-alanine has been identified in the human placenta (PMID: 32033212). N-Acetyl-L-alanine is a substrate for Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit, Myelin basic protein, GTP-binding nuclear protein Ran, Tropomyosin alpha 4 chain, HIV-1 Rev binding protein 2, Xaa-Pro dipeptidase, Thymosin beta-10, Actin-like protein 3, Alanine aminotransferase, Serine/threonine protein phosphatase PP1-beta catalytic subunit, 10 kDa heat shock protein (mitochondrial), Calmodulin and Beta-1-syntrophin. [HMDB] C26170 - Protective Agent > C275 - Antioxidant Ac-Ala-OH is an endogenous metabolite.
N-acetylarginine
N-alpha-Acetyl-L-arginine, also known as N-alpha-acetylarginine, 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-Acetylarginine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetylarginine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-arginine. 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-acetylarginine 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 arginine can also occur. Many N-acetylamino acids, including N-acetylarginine are classified as uremic toxins if present in high abundance in the serum or plasma (PMID: 26317986; PMID: 20613759; PMID: 7777105). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). N-alpha-Acetyl-L-arginine serum levels (and other guanidino compounds) were elevated of all the hyperargininemic patients are higher than the normal range. Untreated hyperargininemic patients have the highest guanidino compound levels in cerebrospinal fluid. N-alpha-Acetyl-L-arginine is also increased in the urine or hyperargininemic patients. N-alpha-Acetyl-L-arginine is one of the guanidino compounds found elevated in the serum of hemodialyzed renal insufficient (uremic) pediatric patients. N-alpha-Acetylarginine is one of the guanidino compounds found elevated in the serum of an hemodialyzed renal insufficient (uremic) pediatric population. (PMID 7777105) N-Acetyl-L-arginine (Ac-Arg-OH) is one of the guanidino compounds found elevated in the serum of an hemodialyzed renal insufficient (uremic) pediatric population.
N-Acetylthreonine
N-Acetyl-L-threonine (or N-Acetylthreonine, 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-Acetylthreonine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetylthreonine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-threonine. 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-acetylthreonine 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 threonine can also occur. Excessive amounts N-acetyl amino acids including N-acetylthreonine (as well as N-acetylglycine, N-acetylserine, N-acetylmethionine, N-acetylglutamate, N-acetylalanine, N-acetylleucine and smaller amounts of N-acetylglutamine, N-acetylisoleucine, and N-acetylvaline) can be detected in the urine with individuals with acylase I deficiency, a genetic disorder (PMID: 16465618). 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 will experience convulsions, hearing loss and difficulty feeding (PMID: 16465618). ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. Many N-acetylamino acids, including N-acetylthreonine are classified as uremic toxins if present in high abundance in the serum or plasma (PMID: 26317986; PMID: 20613759). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). N-Acetylthreonine has been identified in the human placenta (PMID: 32033212).
Isovalerylalanine
Isovalerylalanine, also known as isopentanoylalanine, 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. Isovalerylalanine results from the formal condensation of the carboxy group of isovaleric acid with the amino group of L-alanine. Isovalerylalanine is one of the constituents of the organic acid profile in isovaleric acidemia, it is believed to be formed by the action of the enzyme glycine N-acylase on alanine, using isovaleryl-CoA as a substrate (PMID: 6197208). Isovaleric acidemia was the first organic acid acidemia to be documented in humans. It is an autosomal recessive inborn error in the metabolism of leucine, caused by a deficiency of the mitochondrial enzyme isovaleryl-CoA dehydrogenase (IVD) that results in the accumulation isovaleryl-CoA derivatives (PMID: 16602101). The excess of isovaleryl-CoA in plasma allows for the formation of condensation derivatives, such as isovalerylalanine which makes it one of the biomarkers for this condition. Isovalerylalanine is a metabolite
N-acetyl-S-(3-oxo-3-carboxy-n-propyl)cysteine
N-acetyl-S-(3-oxo-3-carboxy-n-propyl)cysteine is a cystathione metabolite found in the urine of patients with cystathionuria (PMID 8750604 ). A cystathione metabolite found in the urine of patients with cystathionuria (PMID 8750604 ) [HMDB]
1-(Malonylamino)cyclopropanecarboxylic acid
1-(Malonylamino)cyclopropanecarboxylic acid is found in cereals and cereal products. 1-(Malonylamino)cyclopropanecarboxylic acid is a constituent of numerous plant species including wheat, tomato and sweet corn Constituent of numerous plant subspecies including wheat, tomato and sweet corn. 1-(Malonylamino)cyclopropanecarboxylic acid is found in cereals and cereal products and garden tomato.
N-Propionylalanine
N-propionylalanine is classified as a member of the n-acyl-l-alpha-amino acids. N-acyl-L-alpha-amino acids are n-acylated alpha amino acids which have the L-configuration of the alpha-carbon atom. N-propionylalanine is considered to be a slightly soluble (in water) and a weak acidic compound. N-propionylalanine can be found in humans.
N-Acetylmethionine sulfoxide
N-Acetylmethionine sulfoxide (CAS: 3054-51-1), also known as N-ACMSO or 2-(acetylamino)-4-(methylsulfinyl)butanoic acid, 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-Acetylmethionine sulfoxide has been identified in the human placenta (PMID: 32033212).
N2,N5-Diacetylornithine
N2,N5-Diacetylornithine, also known as bisorcic, 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. N2,N5-Diacetylornithine is an N-acetyl-L-amino acid that is L-ornithine carrying two acetyl substituents at positions N-2 and N-5. N2,N5-Diacetylornithine was identified as one of forty plasma metabolites that could be used to predict gut microbiome Shannon diversity (PMID: 31477923). Shannon diversity is a metric that summarizes both species abundance and evenness, and it has been suggested as a marker for microbiome health. C78272 - Agent Affecting Nervous System > C29710 - Antipsychotic Agent
