Beta-aminoglutaric acid (BAG) is a non-proteinogenic amino acid that has been shown to be involved in several metabolic pathways. BAG is a precursor to the neurotransmitter GABA, and it has been shown to have neuroprotective effects in animal models of stroke and Alzheimer's disease. It is synthesized in the body from glutamate. The synthesis of beta-aminoglutaric acid involves a multi-step process that begins with the decarboxylation of glutamate to form gamma-aminobutyrate (GABA). GABA is then converted to beta-aminoglutaric acid by the enzyme GABA transaminase. Studies have shown that beta-aminoglutaric acid may play a role in the regulation of brain function, and it has been suggested as a potential therapeutic agent for the treatment of neurological disorders. The effects of BAG have been studied in relation to its potential role in the treatment of neurological disorders, such as Alzheimer's disease, Parkinson's disease, and epilepsy. It has also been studied for its potential as a treatment for cardiovascular disease and cancer. Its potential for regulating neurological pathways has made it a target for scientific research.'
3-aminoglutaric acid: RN given refers to parent cpd; structure given in first source
isoglutamic acid : A 1,5-dicarboxylic acid compound having a 3-amino substituent. It has been isolated from the extracts of the algae, Chondria armata.
ID Source | ID |
---|---|
PubMed CID | 73064 |
CHEBI ID | 28791 |
SCHEMBL ID | 288510 |
MeSH ID | M0108172 |
Synonym |
---|
beta glutamic acid |
nsc-341646 |
pentanedioic acid, 3-amino- |
1948-48-7 |
glutamic acid, beta |
NSC341646 , |
3-aminopentanedioic acid |
C05574 |
isoglutamic acid |
beta-glutamic acid |
beta-aminoglutaric acid |
3-azanylpentanedioic acid |
3-aminoglutaric acid |
CHEBI:28791 |
3-aminoglutarate |
FT-0650581 |
AKOS006282078 |
unii-sfg5x9c3dq |
sfg5x9c3dq , |
nsc 341646 |
bdbm92996 |
SCHEMBL288510 |
BBJIPMIXTXKYLZ-UHFFFAOYSA-N |
W-204212 |
FD10075 |
DTXSID30173130 |
i(2)-glutamic acid |
mfcd00056698 |
beta-homoasparticacid |
b-glutamic acid |
beta-homoaspartate |
SY239922 |
DS-16434 |
Q27103900 |
A880177 |
3-aminopentanedioicacid |
(2)-glutamic acid |
BAA94848 |
CS-0161137 |
.beta.-aminoglutaric acid |
.beta.-glutamic acid |
EN300-109490 |
Role | Description |
---|---|
marine metabolite | Any metabolite produced during a metabolic reaction in marine macro- and microorganisms. |
algal metabolite | Any eukaryotic metabolite produced during a metabolic reaction in algae including unicellular organisms like chlorella and diatoms to multicellular organisms like giant kelps and brown algae. |
[role information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res] |
Class | Description |
---|---|
dicarboxylic acid | Any carboxylic acid containing two carboxy groups. |
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res] |
Protein | Taxonomy | Measurement | Average | Min (ref.) | Avg (ref.) | Max (ref.) | Bioassay(s) |
---|---|---|---|---|---|---|---|
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023] |
Process | via Protein(s) | Taxonomy |
---|---|---|
aspartate kinase activity | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
homoserine dehydrogenase activity | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
ATP binding | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
kinase activity | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
oxidoreductase activity | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
identical protein binding | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
metal ion binding | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
NADP binding | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
NAD+ binding | Bifunctional aspartokinase/homoserine dehydrogenase 1 | Escherichia coli K-12 |
[Information is prepared from geneontology information from the June-17-2024 release] |
Assay ID | Title | Year | Journal | Article |
---|---|---|---|---|
AID1799870 | Inhibition Assay from Article 10.1021/bi00118a023: \\Reversal of enzyme regiospecificity with alternative substrates for aspartokinase I from Escherichia coli.\\ | 1992 | Biochemistry, Jan-28, Volume: 31, Issue:3 | Reversal of enzyme regiospecificity with alternative substrates for aspartokinase I from Escherichia coli. |
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] |
Timeframe | Studies, This Drug (%) | All Drugs % |
---|---|---|
pre-1990 | 6 (42.86) | 18.7374 |
1990's | 3 (21.43) | 18.2507 |
2000's | 2 (14.29) | 29.6817 |
2010's | 3 (21.43) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023] |
According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be weak demand-to-supply ratio for research on this compound.
| This Compound (11.79) All Compounds (24.57) |
Publication Type | This drug (%) | All Drugs (%) |
---|---|---|
Trials | 0 (0.00%) | 5.53% |
Reviews | 0 (0.00%) | 6.00% |
Case Studies | 0 (0.00%) | 4.05% |
Observational | 0 (0.00%) | 0.25% |
Other | 14 (100.00%) | 84.16% |
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023] |