Page last updated: 2024-12-05

3-methyl-1,2-cyclopentanedione

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

Description

cyclotene: product of sugar degradation [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

3-methyl-1,2-cyclopentanedione: a peroxynitrite scavenger isolated from coffee extract; structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID6660
SCHEMBL ID112009
MeSH IDM0446544
PubMed CID61209
CHEMBL ID371371
CHEBI ID173373
SCHEMBL ID511158
MeSH IDM0446544

Synonyms (89)

Synonym
80-71-7
nsc133445
2-cyclopenten-1-one, 2-hydroxy-3-methyl-
cyclotene
nsc-133445
2-hydroxy-1-methylcyclopenten-3-one
corylone
corylon
cycloten
NCIOPEN2_001017
2-hydroxy-3-methyl-2-cyclopentenone
epa pesticide chemical code 004049
3-methylcyclopent-2-en-2-ol-1-one
cyclotene (ordorant)
3-methyl-2-hydroxy-2-cyclopentenone
einecs 201-303-2
3-methyl-2-cyclopentene-2-ol-1-one
maple lactone
ai3-36598
brn 2039308
ccris 2940
nsc 133445
2-hydroxy-3-methylcyclopent-2-enone
2-hydroxy-3-methyl-2-cyclopenten-1-one
2-hydroxy-3-methyl-cyclopent-2-en-1-one
nsc-84226
nsc84226
inchi=1/c6h8o2/c1-4-2-3-5(7)6(4)8/h8h,2-3h2,1h
2-hydroxy-3-methylcyclopent-2-en-1-one
3-methyl-2-cyclopentenon-2-ol
H0469
A839968
methyl cyclopentenolone
unii-627e92x64b
627e92x64b ,
AKOS015960664
FT-0628871
SCHEMBL112009
methylcyclopentenolone [fhfi]
3-methyl-2-cyclopenten-2-ol-1-one
methyl cyclopentenolone [fcc]
AKOS025243271
mfcd00013747
DS-2505
Q-100838
2-hydroxy-3-methyl-2-cyclopentene-1-one
CFAKWWQIUFSQFU-UHFFFAOYSA-N
cyclotene (odorant)
DTXSID4035128
Z1483987834
2-hydroxy-3-methyl-cyclopent-2-enone
2-cyclopenten-1-one,2-hydroxy-3-methyl-
Q25101336
EN300-113773
O10798
CS-W013661
CHEBI:173373
765-70-8
3-methyl-1,2-cyclopentanedione
1,2-cyclopentanedione, 3-methyl-
bdbm22767
methylcyclopentenolone (natural)
methylcyclopentenolone (diketo form)
einecs 212-154-8
3-methylcyclopentane-1,2-dione
3-methyl-1,2-cyclopentanedione, 99%
CHEMBL371371
STK801987
AKOS000119750
tox21_302629
NCGC00256786-01
dtxcid2027709
cas-765-70-8
dtxsid3047716 ,
FT-0616152
SCHEMBL511158
W-104356
STR04813
mfcd00001417
3-methyl-1,2-cyclopentanedione, 98%
2-hydroxy-5-methyl-2-cyclopenten-1-one
fema 2700
methyl-cyclopentenolone
methyl cyclopentenlone
E75724
M2904
3-methyl-1.2-cyclopentanedione
AKOS016843942
CS-W011271
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Drug Classes (1)

ClassDescription
cyclic ketone
[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 (7)

Potency Measurements

ProteinTaxonomyMeasurementAverage (µ)Min (ref.)Avg (ref.)Max (ref.)Bioassay(s)
estrogen nuclear receptor alphaHomo sapiens (human)Potency30.57170.000229.305416,493.5996AID743078
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
Cocaine esteraseHomo sapiens (human)Ki100.00000.00630.98358.0000AID239272
Coagulation factor XIIHomo sapiens (human)Ki83.14000.00251.86697.2500AID1798224
CholinesteraseHomo sapiens (human)Ki85.95000.00001.51739.7300AID1798224; AID239166
Liver carboxylesterase 1Oryctolagus cuniculus (rabbit)Ki71.90000.01361.70257.2500AID1798224; AID239167
AcetylcholinesteraseHomo sapiens (human)Ki85.95000.00001.27869.7300AID1798224; AID239122
Liver carboxylesterase 1Homo sapiens (human)Ki85.95000.00252.01368.4800AID1798224; AID239197
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (56)

Processvia Protein(s)Taxonomy
prostaglandin metabolic processCocaine esteraseHomo sapiens (human)
xenobiotic metabolic processCocaine esteraseHomo sapiens (human)
catabolic processCocaine esteraseHomo sapiens (human)
plasma kallikrein-kinin cascadeCoagulation factor XIIHomo sapiens (human)
Factor XII activationCoagulation factor XIIHomo sapiens (human)
blood coagulation, intrinsic pathwayCoagulation factor XIIHomo sapiens (human)
positive regulation of plasminogen activationCoagulation factor XIIHomo sapiens (human)
protein processingCoagulation factor XIIHomo sapiens (human)
protein autoprocessingCoagulation factor XIIHomo sapiens (human)
positive regulation of blood coagulationCoagulation factor XIIHomo sapiens (human)
zymogen activationCoagulation factor XIIHomo sapiens (human)
fibrinolysisCoagulation factor XIIHomo sapiens (human)
innate immune responseCoagulation factor XIIHomo sapiens (human)
response to misfolded proteinCoagulation factor XIIHomo sapiens (human)
positive regulation of fibrinolysisCoagulation factor XIIHomo sapiens (human)
blood coagulationCoagulation factor XIIHomo sapiens (human)
xenobiotic metabolic processCholinesteraseHomo sapiens (human)
learningCholinesteraseHomo sapiens (human)
negative regulation of cell population proliferationCholinesteraseHomo sapiens (human)
neuroblast differentiationCholinesteraseHomo sapiens (human)
peptide hormone processingCholinesteraseHomo sapiens (human)
response to alkaloidCholinesteraseHomo sapiens (human)
cocaine metabolic processCholinesteraseHomo sapiens (human)
negative regulation of synaptic transmissionCholinesteraseHomo sapiens (human)
response to glucocorticoidCholinesteraseHomo sapiens (human)
response to folic acidCholinesteraseHomo sapiens (human)
choline metabolic processCholinesteraseHomo sapiens (human)
acetylcholine catabolic processCholinesteraseHomo sapiens (human)
acetylcholine catabolic process in synaptic cleftAcetylcholinesteraseHomo sapiens (human)
regulation of receptor recyclingAcetylcholinesteraseHomo sapiens (human)
osteoblast developmentAcetylcholinesteraseHomo sapiens (human)
acetylcholine catabolic processAcetylcholinesteraseHomo sapiens (human)
cell adhesionAcetylcholinesteraseHomo sapiens (human)
nervous system developmentAcetylcholinesteraseHomo sapiens (human)
synapse assemblyAcetylcholinesteraseHomo sapiens (human)
receptor internalizationAcetylcholinesteraseHomo sapiens (human)
negative regulation of synaptic transmission, cholinergicAcetylcholinesteraseHomo sapiens (human)
amyloid precursor protein metabolic processAcetylcholinesteraseHomo sapiens (human)
positive regulation of protein secretionAcetylcholinesteraseHomo sapiens (human)
retina development in camera-type eyeAcetylcholinesteraseHomo sapiens (human)
acetylcholine receptor signaling pathwayAcetylcholinesteraseHomo sapiens (human)
positive regulation of cold-induced thermogenesisAcetylcholinesteraseHomo sapiens (human)
cholesterol biosynthetic processLiver carboxylesterase 1Homo sapiens (human)
cholesterol metabolic processLiver carboxylesterase 1Homo sapiens (human)
response to toxic substanceLiver carboxylesterase 1Homo sapiens (human)
positive regulation of cholesterol effluxLiver carboxylesterase 1Homo sapiens (human)
negative regulation of cholesterol storageLiver carboxylesterase 1Homo sapiens (human)
epithelial cell differentiationLiver carboxylesterase 1Homo sapiens (human)
cholesterol homeostasisLiver carboxylesterase 1Homo sapiens (human)
reverse cholesterol transportLiver carboxylesterase 1Homo sapiens (human)
medium-chain fatty acid metabolic processLiver carboxylesterase 1Homo sapiens (human)
regulation of bile acid biosynthetic processLiver carboxylesterase 1Homo sapiens (human)
cellular response to cholesterolLiver carboxylesterase 1Homo sapiens (human)
cellular response to low-density lipoprotein particle stimulusLiver carboxylesterase 1Homo sapiens (human)
cholesterol ester hydrolysis involved in cholesterol transportLiver carboxylesterase 1Homo sapiens (human)
positive regulation of cholesterol metabolic processLiver carboxylesterase 1Homo sapiens (human)
regulation of bile acid secretionLiver carboxylesterase 1Homo sapiens (human)
lipid catabolic processLiver carboxylesterase 1Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (22)

Processvia Protein(s)Taxonomy
methylumbelliferyl-acetate deacetylase activityCocaine esteraseHomo sapiens (human)
carboxylesterase activityCocaine esteraseHomo sapiens (human)
carboxylic ester hydrolase activityCocaine esteraseHomo sapiens (human)
serine-type endopeptidase activityCoagulation factor XIIHomo sapiens (human)
calcium ion bindingCoagulation factor XIIHomo sapiens (human)
protein bindingCoagulation factor XIIHomo sapiens (human)
misfolded protein bindingCoagulation factor XIIHomo sapiens (human)
amyloid-beta bindingCholinesteraseHomo sapiens (human)
catalytic activityCholinesteraseHomo sapiens (human)
acetylcholinesterase activityCholinesteraseHomo sapiens (human)
cholinesterase activityCholinesteraseHomo sapiens (human)
protein bindingCholinesteraseHomo sapiens (human)
hydrolase activity, acting on ester bondsCholinesteraseHomo sapiens (human)
enzyme bindingCholinesteraseHomo sapiens (human)
choline bindingCholinesteraseHomo sapiens (human)
identical protein bindingCholinesteraseHomo sapiens (human)
amyloid-beta bindingAcetylcholinesteraseHomo sapiens (human)
acetylcholinesterase activityAcetylcholinesteraseHomo sapiens (human)
cholinesterase activityAcetylcholinesteraseHomo sapiens (human)
protein bindingAcetylcholinesteraseHomo sapiens (human)
collagen bindingAcetylcholinesteraseHomo sapiens (human)
hydrolase activityAcetylcholinesteraseHomo sapiens (human)
serine hydrolase activityAcetylcholinesteraseHomo sapiens (human)
acetylcholine bindingAcetylcholinesteraseHomo sapiens (human)
protein homodimerization activityAcetylcholinesteraseHomo sapiens (human)
laminin bindingAcetylcholinesteraseHomo sapiens (human)
sterol esterase activityLiver carboxylesterase 1Homo sapiens (human)
methylumbelliferyl-acetate deacetylase activityLiver carboxylesterase 1Homo sapiens (human)
carboxylesterase activityLiver carboxylesterase 1Homo sapiens (human)
carboxylic ester hydrolase activityLiver carboxylesterase 1Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (24)

Processvia Protein(s)Taxonomy
endoplasmic reticulumCocaine esteraseHomo sapiens (human)
endoplasmic reticulum lumenCocaine esteraseHomo sapiens (human)
intracellular membrane-bounded organelleCocaine esteraseHomo sapiens (human)
extracellular regionCoagulation factor XIIHomo sapiens (human)
extracellular spaceCoagulation factor XIIHomo sapiens (human)
plasma membraneCoagulation factor XIIHomo sapiens (human)
collagen-containing extracellular matrixCoagulation factor XIIHomo sapiens (human)
extracellular exosomeCoagulation factor XIIHomo sapiens (human)
extracellular spaceCoagulation factor XIIHomo sapiens (human)
rough endoplasmic reticulumCoagulation factor XIIHomo sapiens (human)
extracellular regionCholinesteraseHomo sapiens (human)
nuclear envelope lumenCholinesteraseHomo sapiens (human)
endoplasmic reticulum lumenCholinesteraseHomo sapiens (human)
blood microparticleCholinesteraseHomo sapiens (human)
plasma membraneCholinesteraseHomo sapiens (human)
extracellular spaceCholinesteraseHomo sapiens (human)
extracellular regionAcetylcholinesteraseHomo sapiens (human)
basement membraneAcetylcholinesteraseHomo sapiens (human)
extracellular spaceAcetylcholinesteraseHomo sapiens (human)
nucleusAcetylcholinesteraseHomo sapiens (human)
Golgi apparatusAcetylcholinesteraseHomo sapiens (human)
plasma membraneAcetylcholinesteraseHomo sapiens (human)
cell surfaceAcetylcholinesteraseHomo sapiens (human)
membraneAcetylcholinesteraseHomo sapiens (human)
neuromuscular junctionAcetylcholinesteraseHomo sapiens (human)
synaptic cleftAcetylcholinesteraseHomo sapiens (human)
synapseAcetylcholinesteraseHomo sapiens (human)
perinuclear region of cytoplasmAcetylcholinesteraseHomo sapiens (human)
side of membraneAcetylcholinesteraseHomo sapiens (human)
cytoplasmLiver carboxylesterase 1Homo sapiens (human)
endoplasmic reticulumLiver carboxylesterase 1Homo sapiens (human)
endoplasmic reticulum lumenLiver carboxylesterase 1Homo sapiens (human)
lipid dropletLiver carboxylesterase 1Homo sapiens (human)
cytosolLiver carboxylesterase 1Homo sapiens (human)
lipid dropletLiver carboxylesterase 1Homo sapiens (human)
endoplasmic reticulumLiver carboxylesterase 1Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (6)

Assay IDTitleYearJournalArticle
AID239272Inhibition constant against human intestinal carboxylesterase 2 (hiCE) using nitrophenyl acetate (o-NPA) as substrate2005Journal of medicinal chemistry, Apr-21, Volume: 48, Issue:8
Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.
AID239122Inhibition constant against human Acetylcholinesterase (hAcChE) using acetylthiocholine (AcTCh) as substrate2005Journal of medicinal chemistry, Apr-21, Volume: 48, Issue:8
Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.
AID239197Inhibition constant against human liver carboxylesterase 1 (hCE1) using nitrophenyl acetate (o-NPA) as substrate2005Journal of medicinal chemistry, Apr-21, Volume: 48, Issue:8
Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.
AID239167Inhibition constant against rabbit liver carboxylesterase (rCE) using nitrophenyl acetate (o-NPA) as substrate2005Journal of medicinal chemistry, Apr-21, Volume: 48, Issue:8
Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.
AID239166Inhibition constant against human Butyrylcholinesterase (hBuChE) using butyrylthiocholine (BuTCh) as substrate2005Journal of medicinal chemistry, Apr-21, Volume: 48, Issue:8
Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.
AID1798224Enzyme Inhibition Assay from Article 10.1021/jm049011j: \\Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.\\2005Journal of medicinal chemistry, Apr-21, Volume: 48, Issue:8
Identification and characterization of novel benzil (diphenylethane-1,2-dione) analogues as inhibitors of mammalian carboxylesterases.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (12)

TimeframeStudies, This Drug (%)All Drugs %
pre-19901 (8.33)18.7374
1990's1 (8.33)18.2507
2000's7 (58.33)29.6817
2010's2 (16.67)24.3611
2020's1 (8.33)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 37.44

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 strong demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index37.44 (24.57)
Research Supply Index2.20 (2.92)
Research Growth Index4.80 (4.65)
Search Engine Demand Index43.55 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (37.44)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Trials0 (0.00%)5.53%
Reviews1 (12.50%)6.00%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Observational0 (0.00%)0.25%
Other7 (87.50%)84.16%
Other5 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]