Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Homo sapiens Reaction: 2.1.1.6

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

EC Number: 2.1.1.6

Enzymes and Genes:
catechol O-methyltransferase : COMT
transmembrane O-methyltransferase : LRTOMT

In Pathway: dopamine degradation

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

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.

Direct generic reaction:
a catechol + S-adenosyl-L-methionine → a guaiacol + S-adenosyl-L-homocysteine + H+ (2.1.1.6)

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

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

Citations: [Axelrod58, Gulliver79, Huh79]

Gene-Reaction Schematic: ?

Instance reactions of [a catechol + S-adenosyl-L-methionine → a guaiacol + S-adenosyl-L-homocysteine + H+] (2.1.1.6):
i1: 3,4-dihydroxyphenylglycol + S-adenosyl-L-methionine → 3-methoxy-4-hydroxyphenylglycol + S-adenosyl-L-homocysteine + H+ (2.1.1.6)

i2: 3,4-dihydroxymandelate + S-adenosyl-L-methionine → vanillyl mandelate + S-adenosyl-L-homocysteine + H+ (2.1.1.6)

i3: 3,4-dihydroxyphenylacetate + S-adenosyl-L-methionine → homovanillate + S-adenosyl-L-homocysteine + H+ (2.1.1.6)
i4: S-adenosyl-L-methionine + dopamine → S-adenosyl-L-homocysteine + 3-methoxytyramine + H+ (2.1.1.6)

i5: (R)-adrenaline + S-adenosyl-L-methionine → metanephrine + S-adenosyl-L-homocysteine + H+ (2.1.1.6)

i6: (R)-noradrenaline + S-adenosyl-L-methionine → normetanephrine + S-adenosyl-L-homocysteine + H+ (2.1.1.6)

i7: L-dopa + S-adenosyl-L-methionine → 3-O-methyldopa + S-adenosyl-L-homocysteine + H+ (2.1.1.6)

Relationship Links: BRENDA:EC:2.1.1.6 , ENZYME:EC:2.1.1.6 , IUBMB-ExplorEnz:EC:2.1.1.6


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of HumanCyc: Genome Biology 6(1):1-17 2004
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, BIOCYC13A.