F
IPR014369

Glycine/Sarcosine N-methyltransferase

InterPro entry
Short nameGly/Sar_N_MeTrfase
Overlapping
homologous
superfamilies
 

Description

Glycine/Sarcosine N-methyltransferase catalyses the methylation of glycine, sarcosine and dimethylglycine to sarcosine, dimethylglycine and betaine, respectively, with S-adenosylmethionine (AdoMet) acting as the methyl donor
[7, 6, 3, 4]
.

Methyltransferases (EC
2.1.1.-
) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule
[2, 1, 5]
. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM
[8]
. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids
[2, 1, 8]
. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing
[2, 1, 5]
. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.

References

1.Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome. Wlodarski T, Kutner J, Towpik J, Knizewski L, Rychlewski L, Kudlicki A, Rowicka M, Dziembowski A, Ginalski K. PLoS ONE 6, e23168, (2011). View articlePMID: 21858014

2.Natural history of S-adenosylmethionine-binding proteins. Kozbial PZ, Mushegian AR. BMC Struct. Biol. 5, 19, (2005). View articlePMID: 16225687

3.Mammalian glycine N-methyltransferases. Comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig livers. Ogawa H, Gomi T, Fujioka M. Comp. Biochem. Physiol., B 106, 601-11, (1993). PMID: 8281755

4.Identification of glycine betaine as compatible solute in Synechococcus sp. WH8102 and characterization of its N-methyltransferase genes involved in betaine synthesis. Lu WD, Chi ZM, Su CD. Arch. Microbiol. 186, 495-506, (2006). View articlePMID: 17019606

5.Many paths to methyltransfer: a chronicle of convergence. Schubert HL, Blumenthal RM, Cheng X. Trends Biochem. Sci. 28, 329-35, (2003). View articlePMID: 12826405

6.Destabilization of human glycine N-methyltransferase by H176N mutation. Luka Z, Pakhomova S, Luka Y, Newcomer ME, Wagner C. Protein Sci. 16, 1957-64, (2007). View articlePMID: 17660255

7.Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes. Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME. Proteins 57, 331-7, (2004). View articlePMID: 15340920

8.Universal catalytic domain structure of AdoMet-dependent methyltransferases. Schluckebier G, O'Gara M, Saenger W, Cheng X. J. Mol. Biol. 247, 16-20, (1995). View articlePMID: 7897657

GO terms

biological process

  • None

cellular component

  • None

Cross References

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