Page last updated: 2024-12-06

beta-aminoglutaric acid

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth Market Indicators

Description

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 [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

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. [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]

Cross-References

ID SourceID
PubMed CID73064
CHEBI ID28791
SCHEMBL ID288510
MeSH IDM0108172

Synonyms (42)

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
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Roles (2)

RoleDescription
marine metaboliteAny metabolite produced during a metabolic reaction in marine macro- and microorganisms.
algal metaboliteAny 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]

Drug Classes (1)

ClassDescription
dicarboxylic acidAny 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 Targets (1)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (7)

Processvia Protein(s)Taxonomy
lysine biosynthetic process via diaminopimelateBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
homoserine biosynthetic processBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
protein homotetramerizationBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
aspartate family amino acid biosynthetic processBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
lysine biosynthetic processBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
methionine biosynthetic processBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
threonine biosynthetic processBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
lysine biosynthetic process via diaminopimelateBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
homoserine biosynthetic processBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (9)

Processvia Protein(s)Taxonomy
aspartate kinase activityBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
homoserine dehydrogenase activityBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
ATP bindingBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
kinase activityBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
oxidoreductase activityBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
identical protein bindingBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
metal ion bindingBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
NADP bindingBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
NAD+ bindingBifunctional aspartokinase/homoserine dehydrogenase 1Escherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (1)

Assay IDTitleYearJournalArticle
AID1799870Inhibition Assay from Article 10.1021/bi00118a023: \\Reversal of enzyme regiospecificity with alternative substrates for aspartokinase I from Escherichia coli.\\1992Biochemistry, 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]

Research

Studies (14)

TimeframeStudies, This Drug (%)All Drugs %
pre-19906 (42.86)18.7374
1990's3 (21.43)18.2507
2000's2 (14.29)29.6817
2010's3 (21.43)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 11.79

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.

MetricThis Compound (vs All)
Research Demand Index11.79 (24.57)
Research Supply Index2.71 (2.92)
Research Growth Index4.49 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (11.79)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other14 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]