|PROSITE documentation PDOC00844
NNMT/PNMT/TEMT family of methyltransferases signature
The following cytoplasmic vertebrate methyltransferases are evolutionary
- Nicotinamide N-methyltransferase (EC 126.96.36.199) (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
- Phenylethanolamine N-methyltransferase (EC 188.8.131.52) (PNMT). PNMT catalyzes
the last step in catecholamine biosynthesis, the conversion of noradrenalin
- Indolethylamine N-methyltransferase (EC 184.108.40.206) (INMT).
- Thioether S-methyltransferase (EC 220.127.116.11) (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.
December 2001 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|NNMT_PNMT_TEMT, PS01100; NNMT/PNMT/TEMT family of methyltransferases signature (PATTERN)
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1HNN 1N7I 1N7J 1YZ3 ... [ALL]
||Aksoy S., Szumlanski C.L., Weinshilboum R.M.
||Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization.
||J. Biol. Chem. 269:14835-14840(1994).
||Thompson M.A., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M.
||Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization.
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