Amine N-methyltransferase - Misplaced Pages

Amine N-methyltransferase (EC 2.1.1.49), also called indolethylamine N-methyltransferase, and thioether S-methyltransferase, is an enzyme that is ubiquitously present in non-neural tissues and catalyzes the N-methylation of tryptamine and structurally related compounds. More recently, it was discovered that this enzyme can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.

The chemical reaction taking place is:

S-adenosyl-L-methionine + an amine $\rightleftharpoons$ S-adenosyl-L-homocysteine + a methylated amine

Thus, the two substrates of this enzyme are S-adenosyl methionine and amine, whereas its two products are S-adenosylhomocysteine and methylated amine. In the case of tryptamine and serotonin these then become the dimethylated indolethylamines N,N-dimethyltryptamine (DMT) and bufotenine respectively.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:amine N-methyltransferase. Other names in common use include nicotine N-methyltransferase, tryptamine N-methyltransferase, indolethylamine N-methyltransferase, and arylamine N-methyltransferase. This enzyme participates in tryptophan metabolism.

A wide range of primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2A14.

References

^ tryptamine+N-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Chu, Uyen; Mavlyutov, Timur; Schulman, Amanda; Baker, Erin; Raj, Rebecca; Epstein, Miles; Guo, Lian; Ruoho, Arnold (April 2015). "Methylation of Thiols and Thioethers by Human Indolethylamine-N Methyl Transferase". The FASEB Journal. 29 (S1). doi:10.1096/fasebj.29.1_supplement.1022.7. ISSN 0892-6638.
Mozier, N M; McConnell, K P; Hoffman, J L (April 1988). "S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism". Journal of Biological Chemistry. 263 (10): 4527–4531. doi:10.1016/s0021-9258(18)68814-3. ISSN 0021-9258. PMID 3350800.
J., Kärkkäinen; T. Forsström; J. Tornaeus; K. Wähälä; P. Kiuru; A. Honkanen; U. -H. Stenman; U. Turpeinen; A. Hesso (April 2005). "Potentially hallucinogenic 5-hydroxytryptamine receptor ligands bufotenine and dimethyltryptamine in blood and tissues". Scandinavian Journal of Clinical and Laboratory Investigation. 65 (3): 189–199. doi:10.1080/00365510510013604. PMID 16095048. S2CID 20005294.

Ansher SS, Jakoby WB (1986). "Amine N-methyltransferases from rabbit liver". J. Biol. Chem. 261 (9): 3996–4001. doi:10.1016/S0021-9258(17)35612-0. PMID 3949799.
Crooks PA, Godin CS, Damani LA, Ansher SS, Jakoby WB (1988). "Formation of quaternary amines by N-methylation of azaheterocycles with homogeneous amine N-methyltransferases". Biochem. Pharmacol. 37 (9): 1673–7. doi:10.1016/0006-2952(88)90426-1. PMID 3377829.

External links

EC 2.1.1.49
Lyon ES, Jakoby WB (1981). "Arylamine N-methyltransferase". Detoxication and Drug Metabolism: Conjugation and Related Systems. Methods in Enzymology. Vol. 77. pp. 263–6. doi:10.1016/S0076-6879(81)77035-6. ISBN 9780121819774. PMID 6276654.
Boarder MR, Rodnight R (1976). "Tryptamine-N-methyltransferase activity in brain tissue: a re-examination". Brain Res. 114 (2): 359–64. doi:10.1016/0006-8993(76)90680-6. PMID 963555. S2CID 36334101.

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase
O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase
Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase
Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase Cyclopropane-fatty-acyl-phospholipid synthase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase
Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase
Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase
Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Categories:

Structural studies

See also

References

External links