KEGG   ENZYME: 2.1.1.20Help
Entry
EC 2.1.1.20                 Enzyme                                 

Name
glycine N-methyltransferase;
glycine methyltransferase;
S-adenosyl-L-methionine:glycine methyltransferase;
GNMT
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:glycine N-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine [RN:R00367]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
glycine [CPD:C00037]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
sarcosine [CPD:C00213]
Comment
This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate [4]. Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.8.3, sarcosine dehydrogenase.
History
EC 2.1.1.20 created 1972, modified 2005
Pathway
Glycine, serine and threonine metabolism
Orthology
K00552  
glycine N-methyltransferase
Genes
HSA: 
27232(GNMT)
PTR: 
462703(GNMT)
PPS: 
100993237(GNMT)
GGO: 
101143848(GNMT)
PON: 
100432507(GNMT)
MCC: 
697722(GNMT)
MCF: 
102133929(GNMT)
MMU: 
14711(Gnmt)
RNO: 
25134(Gnmt)
CGE: 
100769585(Gnmt)
HGL: 
101697457(Gnmt)
TUP: 
102501380(GNMT)
CFA: 
474905(GNMT)
AML: 
FCA: 
101083006(GNMT)
PTG: 
102965502(GNMT)
BTA: 
538212(GNMT)
BOM: 
102287446(GNMT)
PHD: 
102315757(GNMT)
CHX: 
102170645(GNMT)
OAS: 
101111134(GNMT)
SSC: 
397444(GNMT)
CFR: 
102506340(GNMT)
BACU: 
103001201(GNMT)
LVE: 
103077097(GNMT)
ECB: 
100067145(GNMT)
MYB: 
102250180(GNMT)
MYD: 
102760706(GNMT)
PALE: 
102898977(GNMT)
MDO: 
100010632(GNMT)
SHR: 
100925098(GNMT)
OAA: 
100681554(GNMT)
MGP: 
TGU: 
FAB: 
101818171(GNMT)
PHI: 
102109993(GNMT)
FPG: 
101921183(GNMT)
FCH: 
102046712(GNMT)
CLV: 
102096572(GNMT)
ASN: 
102386281(GNMT)
AMJ: 
102566047(GNMT)
PSS: 
102460961(GNMT)
CMY: 
102938095(GNMT)
ACS: 
100552842(gnmt)
PBI: 
103067312(GNMT)
XTR: 
DRE: 
403338(gnmt)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103187634(gnmt)
BFO: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
552832(GB16202)
NVI: 
100121709(Gnmt)
TCA: 
BMOR: 
ISC: 
NVE: 
HMG: 
TAD: 
 » show all
Taxonomy
Reference
1  [PMID:13971907]
  Authors
BLUMENSTEIN J, WILLIAMS GR.
  Title
Glycine methyltransferase.
  Journal
Can. J. Biochem. Physiol. 41 (1963) 201-10.
Reference
2  [PMID:9597750]
  Authors
Ogawa H, Gomi T, Takusagawa F, Fujioka M.
  Title
Structure, function and physiological role of glycine N-methyltransferase.
  Journal
Int. J. Biochem. Cell. Biol. 30 (1998) 13-26.
Reference
3  [PMID:10608809]
  Authors
Yeo EJ, Briggs WT, Wagner C.
  Title
Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate.
  Journal
J. Biol. Chem. 274 (1999) 37559-64.
Reference
4  [PMID:10833353]
  Authors
Martinov MV, Vitvitsky VM, Mosharov EV, Banerjee R, Ataullakhanov FI.
  Title
A substrate switch: a new mode of regulation in the methionine metabolic pathway.
  Journal
J. Theor. Biol. 204 (2000) 521-32.
Reference
5  [PMID:12859184]
  Authors
Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F.
  Title
Catalytic mechanism of glycine N-methyltransferase.
  Journal
Biochemistry. 42 (2003) 8394-402.
  Sequence
[rno:25134]
Reference
6  [PMID:15340920]
  Authors
Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME.
  Title
Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.
  Journal
Proteins. 57 (2004) 331-7.
  Sequence
[hsa:27232] [mmu:14711]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37228-72-1

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