KEGG   ENZYME: 2.1.1.6Help
Entry
EC 2.1.1.6                  Enzyme                                 

Name
catechol O-methyltransferase;
COMT I ;
COMT II;
S-COMT (soluble form of catechol-O-methyltransferase);
MB-COMT (membrane-bound form of catechol-O-methyltransferase);
catechol methyltransferase;
catecholamine O-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:catechol O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol [RN:R07330]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
catechol [CPD:C00090]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
guaiacol [CPD:C01502]
Comment
The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols.
History
EC 2.1.1.6 created 1965
Pathway
Steroid hormone biosynthesis
Tyrosine metabolism
Betalain biosynthesis
Metabolic pathways
Orthology
K00545  
catechol O-methyltransferase
Genes
HSA: 
1312(COMT)
PTR: 
458655(COMT)
PPS: 
100982622(COMT)
GGO: 
101134139(COMT)
PON: 
100455627(COMT)
MCC: 
712548(COMT)
MCF: 
102114823(COMT)
MMU: 
12846(Comt)
RNO: 
24267(Comt)
CGE: 
HGL: 
101717730(Comt)
TUP: 
102485737(COMT)
CFA: 
445450(COMT)
FCA: 
101097022(COMT)
PTG: 
102959975(COMT)
BTA: 
618278(COMT)
BOM: 
102271180(COMT)
PHD: 
102320187(COMT)
CHX: 
SSC: 
100155530(COMT)
CFR: 
102522928(COMT)
ECB: 
100146509(COMT)
MYB: 
102256228(COMT)
MYD: 
102753607(COMT)
MDO: 
SHR: 
100934159(COMT)
OAA: 
GGA: 
416783(COMT)
MGP: 
TGU: 
100223814(COMT)
FAB: 
101818536(COMT)
PHI: 
102099819(COMT)
APLA: 
101805407(COMT)
FPG: 
101916407(COMT)
FCH: 
102046620(COMT)
CLV: 
102088102(COMT)
ASN: 
102371384(COMT)
PSS: 
102459109(COMT)
CMY: 
102945092(COMT)
XLA: 
379402(MGC53924)
XTR: 
DRE: 
561372(comta) 565370(comtb)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
SPU: 
SMO: 
PPP: 
OLU: 
OTA: 
MIS: 
DHA: 
PIC: 
PGU: 
LEL: 
CAL: 
CaO19.7140(CMT1) CaO19_7140(CaJ7_0501)
CTP: 
CDU: 
COT: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MGR: 
FGR: 
NHE: 
VAL: 
SSL: 
BFU: 
ANI: 
NFI: 
AFM: 
AOR: 
AOR_1_526114(AO090701000285)
ANG: 
ANI_1_376154(An17g00200)
AFV: 
ACT: 
CIM: 
CPW: 
PBL: 
PNO: 
PTE: 
ZTR: 
SPO: 
PTI: 
TPS: 
PIF: 
EHX: 
GTT: 
MTU: 
MTV: 
MTC: 
MRA: 
MTF: 
MTB: 
MTK: 
MTZ: 
MTG: 
MTI: 
MTE: 
MTUR: 
MTL: 
MTO: 
MTD: 
MTN: 
MTJ: 
MTUB: 
MTUE: 
MTX: 
MTUH: 
MTUL: 
MBO: 
MBB: 
MBT: 
MBM: 
MBK: 
MAF: 
MCE: 
MCQ: 
MCV: 
MCX: 
MCZ: 
MPA: 
MAO: 
MAV: 
MIT: 
MIR: 
MIA: 
MID: 
MYO: 
MSA: 
MUL: 
MVA: 
MGI: 
MSP: 
MAB: 
MABB: 
MJD: 
MMI: 
MRH: 
MMM: 
MLI: 
MKN: 
 » show all
Taxonomy
Reference
1  [PMID:13575440]
  Authors
AXELROD J, TOMCHICK R.
  Title
Enzymatic O-methylation of epinephrine and other catechols.
  Journal
J. Biol. Chem. 233 (1958) 702-5.
  Organism
Rattus norvegicus
Reference
2  [PMID:438821]
  Authors
Gulliver PA, Tipton KF.
  Title
The purification and properties of pig brain catechol-o-methyltransferase.
  Journal
J. Neurochem. 32 (1979) 1525-9.
  Organism
Sus scofa
Reference
3  [PMID:762061]
  Authors
Huh MM, Friedhoff AJ.
  Title
Multiple molecular forms of catechol-O-methyltransferase. Evidence for two distinct forms, and their purification and physical characterization.
  Journal
J. Biol. Chem. 254 (1979) 299-308.
  Organism
Rattus norvegicus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9012-25-3

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