View source for (cytochrome c)-methionine S-methyltransferase

{{enzyme
| Name = glycine N-methyltransferase
| EC_number = 2.1.1.20
| CAS_number = 37228-72-1
| IUBMB_EC_number = 2/1/1/20
| GO_code = 0017174
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''glycine N-methyltransferase''' ({{EC number|2.1.1.20}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:S-adenosyl-L-methionine + glycine <math>\rightleftharpoons</math> S-adenosyl-L-homocysteine + sarcosine

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[S-Adenosyl methionine|S-adenosyl methionine]] and [[glycine]], whereas its two [[product (chemistry)|products]] are [[S-adenosylhomocysteine]] and [[sarcosine]].

This enzyme belongs to the family of [[transferase]]s, specifically those transferring one-carbon group methyltransferases.  The systematic name of this enzyme class is '''S-adenosyl-L-methionine:glycine N-methyltransferase'''. Other names in common use include '''glycine methyltransferase''', '''S-adenosyl-L-methionine:glycine methyltransferase''', and '''GNMT'''.  This enzyme participates in [[glycine, serine and threonine metabolism]].  

==Structural studies==

As of late 2007, 12 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1BHJ}}, {{PDB link|1D2C}}, {{PDB link|1D2G}}, {{PDB link|1D2H}}, {{PDB link|1KIA}}, {{PDB link|1NBH}}, {{PDB link|1NBI}}, {{PDB link|1R74}}, {{PDB link|1XVA}}, {{PDB link|2AZT}}, {{PDB link|2IDJ}}, and {{PDB link|2IDK}}.

==References==
{{reflist|1}}
* {{cite journal | author = BLUMENSTEIN J, WILLIAMS GR | date = 1963 | title = Glycine methyltransferase | journal = Can. J. Biochem. Physiol.  | volume = 41 | pages = 201&ndash;10  | pmid = 13971907 | doi = 10.1139/o63-025 }}
* {{cite journal | author = Ogawa H, Gomi T, Takusagawa F, Fujioka M | date = 1998 | title = Structure, function and physiological role of glycine N-methyltransferase | journal = Int. J. Biochem. Cell. Biol.  | volume = 30 | pages = 13&ndash;26  | pmid = 9597750 | doi = 10.1016/S1357-2725(97)00105-2 | issue = 1 }}
* {{cite journal | author = Yeo EJ, Briggs WT, Wagner C | date = 1999 | title = Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate | journal = J. Biol. Chem.  | volume = 274 | pages = 37559&ndash;64  | pmid = 10608809 | doi = 10.1074/jbc.274.53.37559 | issue = 53 }}
* {{cite journal | author = FI | date = 2000 | title = A substrate switch: a new mode of regulation in the methionine metabolic pathway | journal = J. Theor. Biol.  | volume = 204 | pages = 521&ndash;32  | pmid = 10833353 | doi = 10.1006/jtbi.2000.2035 | last2 = Vitvitsky | first2 = VM | last3 = Mosharov | first3 = EV | last4 = Banerjee | first4 = R | last5 = Ataullakhanov | first5 = FI | issue = 4 }}
* {{cite journal | author = Fujioka M, Takusagawa F | date = 2003 | title = Catalytic mechanism of glycine N-methyltransferase | journal = Biochemistry.  | volume = 42 | pages = 8394&ndash;402  | pmid = 12859184 | doi = 10.1021/bi034245a | issue = 28 }}
* {{cite journal | author = Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME | date = 2004 | title = Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes | journal = Proteins.  | volume = 57 | pages = 331&ndash;7  | pmid = 15340920 | doi = 10.1002/prot.20209 | issue = 2 }}

{{transferase-stub}}

[[Category:EC 2.1.1]]
[[Category:Enzymes of known structure]]