Page last updated: 2024-11-07

agatoxin-489

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

Description

agatoxin-489: structure given in first source; anhydrous MW 489 Da; isolated from Agelenopsis aperta [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID131007
CHEMBL ID3286869
SCHEMBL ID13151437
MeSH IDM0205796

Synonyms (23)

Synonym
1h-indole-3-acetamide, n-(20-amino-4-hydroxy-4,8,12,17-tetraazaeicos-1-yl)-
4q64gnz7kx ,
128549-96-2
n-(20-amino-4-hydroxy-4,8,12,17-tetraazaeicos-1-yl)-1h-indole-3-acetamide
ag-489
ag489
agatoxin-489
unii-4q64gnz7kx
ag 489
n-[3-[3-[3-[4-(3-aminopropylamino)butylamino]propylamino]propyl-hydroxyamino]propyl]-2-(1h-indol-3-yl)acetamide
gtpl2484
agatoxin 489
chembl3286869 ,
bdbm50018845
SCHEMBL13151437
DTXSID40155922
Q4651714
agelenotoxin 489
nps-017
aga-489
.alpha.-agatoxin ag 489
n-[3-(17-amino-1-hydroxy-1,5,9,14-tetraazaheptadecan-1-yl)propyl]-2-(1h-indol-3-yl)acetamide
AKOS040750190
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (5)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Cytochrome P450 3A4Homo sapiens (human)IC50 (µMol)0.01100.00011.753610.0000AID1153200
Glutamate receptor 1Rattus norvegicus (Norway rat)IC50 (µMol)0.01100.00011.617910.0000AID1153200
Glutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)IC50 (µMol)0.01200.00071.600310.0000AID1153199
Glutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)IC50 (µMol)0.01200.00071.630610.0000AID1153199
Prostaglandin D2 receptor 2Homo sapiens (human)IC50 (µMol)0.01200.00040.10090.9600AID1153199
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (27)

Processvia Protein(s)Taxonomy
lipid hydroxylationCytochrome P450 3A4Homo sapiens (human)
lipid metabolic processCytochrome P450 3A4Homo sapiens (human)
steroid catabolic processCytochrome P450 3A4Homo sapiens (human)
xenobiotic metabolic processCytochrome P450 3A4Homo sapiens (human)
steroid metabolic processCytochrome P450 3A4Homo sapiens (human)
cholesterol metabolic processCytochrome P450 3A4Homo sapiens (human)
androgen metabolic processCytochrome P450 3A4Homo sapiens (human)
estrogen metabolic processCytochrome P450 3A4Homo sapiens (human)
alkaloid catabolic processCytochrome P450 3A4Homo sapiens (human)
monoterpenoid metabolic processCytochrome P450 3A4Homo sapiens (human)
calcitriol biosynthetic process from calciolCytochrome P450 3A4Homo sapiens (human)
xenobiotic catabolic processCytochrome P450 3A4Homo sapiens (human)
vitamin D metabolic processCytochrome P450 3A4Homo sapiens (human)
vitamin D catabolic processCytochrome P450 3A4Homo sapiens (human)
retinol metabolic processCytochrome P450 3A4Homo sapiens (human)
retinoic acid metabolic processCytochrome P450 3A4Homo sapiens (human)
long-chain fatty acid biosynthetic processCytochrome P450 3A4Homo sapiens (human)
aflatoxin metabolic processCytochrome P450 3A4Homo sapiens (human)
oxidative demethylationCytochrome P450 3A4Homo sapiens (human)
chemotaxisProstaglandin D2 receptor 2Homo sapiens (human)
immune responseProstaglandin D2 receptor 2Homo sapiens (human)
G protein-coupled receptor signaling pathwayProstaglandin D2 receptor 2Homo sapiens (human)
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathwayProstaglandin D2 receptor 2Homo sapiens (human)
calcium-mediated signalingProstaglandin D2 receptor 2Homo sapiens (human)
positive regulation of G protein-coupled receptor signaling pathwayProstaglandin D2 receptor 2Homo sapiens (human)
negative regulation of male germ cell proliferationProstaglandin D2 receptor 2Homo sapiens (human)
neuropeptide signaling pathwayProstaglandin D2 receptor 2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (28)

Processvia Protein(s)Taxonomy
monooxygenase activityCytochrome P450 3A4Homo sapiens (human)
steroid bindingCytochrome P450 3A4Homo sapiens (human)
iron ion bindingCytochrome P450 3A4Homo sapiens (human)
protein bindingCytochrome P450 3A4Homo sapiens (human)
steroid hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
retinoic acid 4-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
oxidoreductase activityCytochrome P450 3A4Homo sapiens (human)
oxygen bindingCytochrome P450 3A4Homo sapiens (human)
enzyme bindingCytochrome P450 3A4Homo sapiens (human)
heme bindingCytochrome P450 3A4Homo sapiens (human)
vitamin D3 25-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
caffeine oxidase activityCytochrome P450 3A4Homo sapiens (human)
quinine 3-monooxygenase activityCytochrome P450 3A4Homo sapiens (human)
testosterone 6-beta-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
anandamide 8,9 epoxidase activityCytochrome P450 3A4Homo sapiens (human)
anandamide 11,12 epoxidase activityCytochrome P450 3A4Homo sapiens (human)
anandamide 14,15 epoxidase activityCytochrome P450 3A4Homo sapiens (human)
aromatase activityCytochrome P450 3A4Homo sapiens (human)
vitamin D 24-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
estrogen 16-alpha-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
estrogen 2-hydroxylase activityCytochrome P450 3A4Homo sapiens (human)
1,8-cineole 2-exo-monooxygenase activityCytochrome P450 3A4Homo sapiens (human)
prostaglandin J receptor activityProstaglandin D2 receptor 2Homo sapiens (human)
G protein-coupled receptor activityProstaglandin D2 receptor 2Homo sapiens (human)
prostaglandin D receptor activityProstaglandin D2 receptor 2Homo sapiens (human)
prostaglandin F receptor activityProstaglandin D2 receptor 2Homo sapiens (human)
neuropeptide bindingProstaglandin D2 receptor 2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (5)

Processvia Protein(s)Taxonomy
cytoplasmCytochrome P450 3A4Homo sapiens (human)
endoplasmic reticulum membraneCytochrome P450 3A4Homo sapiens (human)
intracellular membrane-bounded organelleCytochrome P450 3A4Homo sapiens (human)
plasma membraneGlutamate receptor 1Rattus norvegicus (Norway rat)
endoplasmic reticulum membraneGlutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)
plasma membraneGlutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Norway rat)
endoplasmic reticulum membraneGlutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)
plasma membraneGlutamate receptor ionotropic, NMDA 2A Rattus norvegicus (Norway rat)
plasma membraneProstaglandin D2 receptor 2Homo sapiens (human)
plasma membraneProstaglandin D2 receptor 2Homo sapiens (human)
neuron projectionProstaglandin D2 receptor 2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (4)

Assay IDTitleYearJournalArticle
AID1346643Rat TRPV1 (Transient Receptor Potential channels)2005Biochemistry, Nov-29, Volume: 44, Issue:47
An inhibitor of TRPV1 channels isolated from funnel Web spider venom.
AID1153199Inhibition of rat recombinant GluN1/2A expressed in Xenopus oocytes assessed as inhibition of glutamate/glycine-evoked channel current at holding potential of -80 mV by two-electrode voltage clamp technique2014Journal of medicinal chemistry, Jun-12, Volume: 57, Issue:11
Structure-activity relationship studies of N-methylated and N-hydroxylated spider polyamine toxins as inhibitors of ionotropic glutamate receptors.
AID1153200Inhibition of rat recombinant GluA1 expressed in Xenopus oocytes assessed as inhibition of glutamate-induced channel current at holding potential of -80 mV by two-electrode voltage clamp technique2014Journal of medicinal chemistry, Jun-12, Volume: 57, Issue:11
Structure-activity relationship studies of N-methylated and N-hydroxylated spider polyamine toxins as inhibitors of ionotropic glutamate receptors.
AID1153198Inhibition of rat recombinant GluN1/2A expressed in Xenopus oocytes assessed as inhibition of glutamate/glycine-evoked channel current at 100 nM at holding potential of -80 mV by two-electrode voltage clamp technique2014Journal of medicinal chemistry, Jun-12, Volume: 57, Issue:11
Structure-activity relationship studies of N-methylated and N-hydroxylated spider polyamine toxins as inhibitors of ionotropic glutamate receptors.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (6)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's2 (33.33)18.2507
2000's2 (33.33)29.6817
2010's2 (33.33)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

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%
Other6 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]