Guanidinoacetate N-methyltransferase
| Guanidinoacetate N-methyltransferase | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 236 amino acids | |
| Secondary to quaternary structure | Monomer | |
| Identifier | ||
| Gene name | GAMT | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 2.1.1.2 , methyltransferase | |
| Response type | (De) methylation | |
| Substrate | S-adenosyl-L-methionine + guanidinoacetate | |
| Products | S-adenosyl-L-homocysteine + creatine | |
| Occurrence | ||
| Homology family | GAMT A | |
| Parent taxon | Newcomers | |
Guanidinoacetate N-methyltransferase (GAMT) is that enzyme , which allows the preparation of creatine from guanidinoacetate catalyzed . Creatine is indispensable as an intermediate energy store in the muscles. Mutations in the GAMT gene can lead to the (rare) GAMT deficiency , which is associated with neurological disorders and muscle hypotonus .
Catalyzed reaction
Guanidinoacetate (from glycine ) is methylated to creatine, whereby S-adenosylmethionine (SAM) provides the transferred methyl group and is itself demethylated to S-adenosyl-L-homocysteine.
Individual evidence
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Arginine Metabolism - Learning and Teaching Materials
