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PROSITE documentation PDOC00844NNMT/PNMT/TEMT family of methyltransferases signature
Description
The following cytoplasmic vertebrate methyltransferases are evolutionary related [1,2]:
- Nicotinamide N-methyltransferase (EC 2.1.1.1) (NNMT). NNMT catalyzes the N- methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for the biotransformation of many drugs and xenobiotic compounds.
- Phenylethanolamine N-methyltransferase (EC 2.1.1.28) (PNMT). PNMT catalyzes the last step in catecholamine biosynthesis, the conversion of noradrenalin to adrenalin.
- Indolethylamine N-methyltransferase (EC 2.1.1.49) (INMT).
- Thioether S-methyltransferase (EC 2.1.1.96) (TEMT). TEMT catalyzes the methylation of dimethyl sulfide into trimethylsulfonium.
These enzymes use S-adenosyl-L-methionine as the methyl donor. They are proteins of 30 to 32 Kd. As a signature pattern we selected the most conserved region, a stretch of 16 residues which are located in the N-terminal section of these enzymes.
Last update:December 2001 / Pattern and text revised.
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Technical section
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References
1 | Authors | Aksoy S. Szumlanski C.L. Weinshilboum R.M. |
Title | Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization. | |
Source | J. Biol. Chem. 269:14835-14840(1994). | |
PubMed ID | 8182091 |
2 | Authors | Thompson M.A. Moon E. Kim U.-J. Xu J. Siciliano M.J. Weinshilboum R.M. |
Title | Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization. | |
Source | Genomics 61:285-297(1999). | |
PubMed ID | 10552930 | |
DOI | 10.1006/geno.1999.5960 |
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