Catechol-O-methyltransferase

COMT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCOMT, HEL-S-98n, catechol-O-methyltransferase
External IDsOMIM: 116790; MGI: 88470; HomoloGene: 30982; GeneCards: COMT; OMA:COMT - orthologs
Orthologs
SpeciesHumanMouse
Entrez

1312

12846

Ensembl

ENSG00000093010

ENSMUSG00000000326

UniProt

P21964

O88587

RefSeq (mRNA)

NM_000754
NM_001135161
NM_001135162
NM_007310
NM_001362828

NM_001111062
NM_001111063
NM_007744

RefSeq (protein)

NP_000745
NP_001128633
NP_001128634
NP_009294
NP_001349757

NP_001104532
NP_001104533
NP_031770

Location (UCSC)Chr 22: 19.94 – 19.97 MbChr 16: 18.23 – 18.25 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse
catechol-O-methyltransferase
Identifiers
EC no.2.1.1.6
CAS no.9012-25-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several enzymes that degrade catecholamines (neurotransmitters such as dopamine, epinephrine, and norepinephrine), catecholestrogens, and various drugs and substances having a catechol structure. In humans, catechol-O-methyltransferase protein is encoded by the COMT gene. Two isoforms of COMT are produced: the soluble short form (S-COMT) and the membrane bound long form (MB-COMT). As the regulation of catecholamines is impaired in a number of medical conditions, several pharmaceutical drugs target COMT to alter its activity and therefore the availability of catecholamines. COMT was first discovered by the biochemist Julius Axelrod in 1957.