MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Instance reactions:
3,4-dihydroxyphenylacetate + S-adenosyl-L-methionine → homovanillate + S-adenosyl-L-homocysteine + H+ (

S-adenosyl-L-methionine + dopamine → S-adenosyl-L-homocysteine + 3-methoxytyramine + H+ (

L-dopa + S-adenosyl-L-methionine → 3-O-methyldopa + S-adenosyl-L-homocysteine + H+ (

(R)-adrenaline + S-adenosyl-L-methionine → metanephrine + S-adenosyl-L-homocysteine + H+ (

(R)-noradrenaline + S-adenosyl-L-methionine → normetanephrine + S-adenosyl-L-homocysteine + H+ (

3,4-dihydroxyphenylglycol + S-adenosyl-L-methionine → 3-methoxy-4-hydroxyphenylglycol + S-adenosyl-L-homocysteine + H+ (

3,4-dihydroxymandelate + S-adenosyl-L-methionine → vanillyl mandelate + S-adenosyl-L-homocysteine + H+ (

Enzyme Commission Primary Name: catechol O-methyltransferase

Enzyme Commission Synonyms: 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

Taxonomic Range: Fungi , Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -24.902267 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The mammalian enzyme acts more rapidly on catecholamines such as adrenaline or noradrenaline than on catechols.

Citations: [Axelrod58, Gulliver79, Huh79]

Unification Links: KEGG:R07330

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC: , UniProt:RELATED-TO:P21964 , UniProt:RELATED-TO:P22734 , UniProt:RELATED-TO:P46484 , UniProt:RELATED-TO:Q04065 , UniProt:RELATED-TO:Q06509 , UniProt:RELATED-TO:Q42949 , UniProt:RELATED-TO:Q42958 , UniProt:RELATED-TO:Q43771 , UniProt:RELATED-TO:Q96565


Axelrod58: Axelrod J, Tomchick R (1958). "Enzymatic O-methylation of epinephrine and other catechols." J Biol Chem 233(3);702-5. PMID: 13575440

Gulliver79: Gulliver PA, Tipton KF (1979). "The purification and properties of pig brain catechol-o-methyltransferase." J Neurochem 32(5);1525-9. PMID: 438821

Huh79: Huh MM, Friedhoff AJ (1979). "Multiple molecular forms of catechol-O-methyltransferase. Evidence for two distinct forms, and their purification and physical characterization." J Biol Chem 254(2);299-308. PMID: 762061

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sat Aug 1, 2015, biocyc14.