ChemFOnt: Showing chemical card for N-Acetyl-L-glutamic acid (CFc000000888)

Record Information

Version

1.0

Creation Date

2022-08-28 10:25:12 UTC

Update Date

2022-09-13 18:45:24 UTC

Chemfont ID

CFc000000888

Molecule Identification

Common Name

N-Acetyl-L-glutamic acid

Definition

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‚Äôs (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 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 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 ).

Structure

MOL SDF PDB SMILES InChI

Synonyms

Value	Source
N-Acetylglutamate	Generator
2-acetamido-L-Glutaraldehydate	HMDB
2-acetamido-L-Glutaraldehydic acid	HMDB
Ac-glu-OH	HMDB
Acetyl-glutamate	HMDB
Acetyl-L-glutamate	HMDB
Acetyl-L-glutamic acid	HMDB
Acetylglutamate	HMDB
Acetylglutamic acid	HMDB
DL-Acetylglutamate	HMDB
DL-Acetylglutamic acid	HMDB
N-Ac-glu-OH	HMDB
N-Acetyl L-glutamate	HMDB
N-Acetyl L-glutamic acid	HMDB
N-Acetyl-DL-glutamate	HMDB
N-Acetyl-DL-glutamic acid	HMDB
N-Acetyl-glutamate	HMDB
N-Acetyl-glutamic acid	HMDB
N-Acetyl-L-glutamate	HMDB
N-Acetyl-L-glutamic acid	HMDB
N-Acetyl-L-glutamic acid-gamma-semialdehyde	HMDB
N-Acetylglutamic gamma-semialdehyde	HMDB

Chemical Formula

C₇H₁₁NO₅

Average Molecular Weight

189.1659

Monoisotopic Molecular Weight

189.063722467

IUPAC Name

2-acetamidopentanedioic acid

Traditional Name

acetylglutamate

CAS Registry Number

1188-37-0

SMILES

CC(O)=NC(CCC(O)=O)C(O)=O

InChI Identifier

InChI=1S/C7H11NO5/c1-4(9)8-5(7(12)13)2-3-6(10)11/h5H,2-3H2,1H3,(H,8,9)(H,10,11)(H,12,13)

InChI Key

RFMMMVDNIPUKGG-UHFFFAOYSA-N

Chemical Taxonomy

Description

Belongs to the class of organic compounds known as glutamic acid and derivatives. Glutamic acid and derivatives 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.

Kingdom

Organic compounds

Super Class

Organic acids and derivatives

Class

Carboxylic acids and derivatives

Sub Class

Amino acids, peptides, and analogues

Direct Parent

Glutamic acid and derivatives

Alternative Parents

Substituents

Glutamic acid or derivatives
N-acyl-alpha-amino acid
N-acyl-alpha amino acid or derivatives
Dicarboxylic acid or derivatives
Fatty acid
Acetamide
Secondary carboxylic acid amide
Carboxamide group
Carboxylic acid
Hydrocarbon derivative
Carbonyl group
Organooxygen compound
Organonitrogen compound
Organic oxygen compound
Organic nitrogen compound
Organopnictogen compound
Organic oxide
Aliphatic acyclic compound

Molecular Framework

Aliphatic acyclic compounds

External Descriptors

Not Available

Functional Ontology

Physiological effect

Not Available

Disposition

Biological location

Non-excretory biofluid

Biofluid or Excreta

Blood (PMID: 32966057)
Saliva (HMDB: HMDB0001138)

Organ

Liver (HMDB: HMDB0001138)
Placenta (HMDB: HMDB0001138)

Excreta

Biofluid or Excreta

Urine (PMID: 19212411)
Feces (PMID: 22411374)

Cellular substructure

Organelle

Mitochondrion (HMDB: HMDB0001138)

Source

Exogenous

Exogenous (HMDB: HMDB0001138)

Endogenous

Endogenous (HMDB: HMDB0001138)

Process

Naturally occurring process

Biological process

Biochemical pathway

Metabolic pathway

Arginine Metabolism (PathBank: SMP0002416)
Proline Metabolism (PathBank: SMP0002420)
Ornithine Metabolism (PathBank: SMP0121275)

Role

Not Available

Physical Properties

Predicted Properties

Property	Value	Source
Water Solubility	5.3 g/L	ALOGPS
logP	-0.48	ALOGPS
logP	-1.1	ChemAxon
logS	-1.6	ALOGPS
pKa (Strongest Acidic)	3.43	ChemAxon
pKa (Strongest Basic)	-1.8	ChemAxon
Physiological Charge	-2	ChemAxon
Hydrogen Acceptor Count	5	ChemAxon
Hydrogen Donor Count	3	ChemAxon
Polar Surface Area	103.7 Å²	ChemAxon
Rotatable Bond Count	5	ChemAxon
Refractivity	40.73 m³·mol⁻¹	ChemAxon
Polarizability	17.28 Å³	ChemAxon
Number of Rings	0	ChemAxon
Bioavailability	Yes	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	No	ChemAxon
Veber's Rule	No	ChemAxon
MDDR-like Rule	No	ChemAxon

External Links

HMDB ID

Not Available

DrugBank ID

Not Available

Phenol Explorer Compound ID

Not Available

FooDB ID

FDB022447

KNApSAcK ID

Not Available

Chemspider ID

Not Available

KEGG Compound ID

Not Available

BioCyc ID

Not Available

BiGG ID

Not Available

Wikipedia Link

N-Acetylglutamic acid

METLIN ID

Not Available

PubChem Compound

185

PDB ID

Not Available

ChEBI ID

Not Available

Food Biomarker Ontology

Not Available

References

Synthesis Reference

hang, Xiaolin; Yang, Qiyong; Sun, Yuesheng. Preparation of N-acetyl-L-glutamic acid. Huaxue Shijie (2002), 43(7), 363-365.

Showing chemical card for N-Acetyl-L-glutamic acid (CFc000000888)

MOL for CFc000000888 (N-Acetyl-L-glutamic acid)

3D MOL for CFc000000888 (N-Acetyl-L-glutamic acid)

3D SDF for CFc000000888 (N-Acetyl-L-glutamic acid)

3D-SDF for CFc000000888 (N-Acetyl-L-glutamic acid)

PDB for CFc000000888 (N-Acetyl-L-glutamic acid)

3D PDB for CFc000000888 (N-Acetyl-L-glutamic acid)

SMILES for CFc000000888 (N-Acetyl-L-glutamic acid)

INCHI for CFc000000888 (N-Acetyl-L-glutamic acid)

Structure for CFc000000888 (N-Acetyl-L-glutamic acid)

3D Structure for CFc000000888 (N-Acetyl-L-glutamic acid)