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
ec00260  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)
NLE: 100603199(GNMT)
MCC: 697722(GNMT)
MCF: 102133929(GNMT)
CSAB: 103221484(GNMT)
RRO: 104667328(GNMT)
RBB: 108533480(GNMT)
CJC: 100413047(GNMT)
SBQ: 101053276(GNMT)
MMU: 14711(Gnmt)
RNO: 25134(Gnmt)
CGE: 100769585(Gnmt)
NGI: 103730804(Gnmt)
HGL: 101697457(Gnmt)
CCAN: 109682081(Gnmt)
OCU: 100009512(GNMT)
TUP: 102501380(GNMT)
CFA: 474905(GNMT)
AML: 100477196(GNMT)
UMR: 103664079(GNMT)
ORO: 101377523(GNMT)
FCA: 101083006(GNMT)
PTG: 102965502(GNMT)
AJU: 106973967(GNMT)
BTA: 538212(GNMT)
BOM: 102287446(GNMT)
BIU: 109577223(GNMT)
PHD: 102315757(GNMT)
CHX: 102170645(GNMT)
OAS: 101111134(GNMT)
SSC: 397444(GNMT)
CFR: 102506340(GNMT)
CDK: 105088648(GNMT)
BACU: 103001201(GNMT)
LVE: 103077097(GNMT)
OOR: 101270773(GNMT)
ECB: 100067145(GNMT)
EPZ: 103548169(GNMT)
EAI: 106828715(GNMT)
MYB: 102250180(GNMT)
MYD: 102760706(GNMT)
HAI: 109382878
RSS: 109450754(GNMT)
PALE: 102898977(GNMT)
LAV: 100660725(GNMT)
TMU: 101355018
MDO: 100010632(GNMT)
SHR: 100925098(GNMT)
OAA: 100681554(GNMT)
GGA: 769542(GNMT)
MGP: 100540940(GNMT)
CJO: 107310908(GNMT)
TGU: 100231507(GNMT)
FAB: 101818171(GNMT)
PHI: 102109993(GNMT)
PMAJ: 107202337(GNMT)
FPG: 101921183(GNMT)
FCH: 102046712(GNMT)
CLV: 102096572
EGZ: 104128772(GNMT)
AAM: 106494152(GNMT)
ASN: 102386281
AMJ: 102566047(GNMT)
PSS: 102460961
CMY: 102938095(GNMT)
CPIC: 101948133(GNMT)
ACS: 100552842(gnmt)
PVT: 110087012(GNMT)
PBI: 103067312(GNMT)
GJA: 107123075(GNMT)
NPR: 108803755
DRE: 403338(gnmt)
SANH: 107697528(gnmt) 107703804
CCAR: 109106978
IPU: 108270118(gnmt)
AMEX: 103028138
TRU: 101067368(gnmt)
LCO: 104932648(gnmt)
NCC: 104954782(gnmt)
MZE: 101484870(gnmt)
OLA: 101154832(gnmt)
XMA: 102219353(gnmt)
NFU: 107389170 107392578(gnmt)
CSEM: 103380842(gnmt)
LCF: 108898000(gnmt)
HCQ: 109530231(gnmt)
BPEC: 110155508(gnmt)
SASA: 106561891(gnmt)
ELS: 105006939(gnmt)
SFM: 108923148
LCM: 102360222(GNMT)
CMK: 103187634(gnmt)
SKO: 100378448
DME: Dmel_CG6188(Gnmt)
DSI: Dsimw501_GD18854(Dsim_GD18854)
MDE: 101892983
AAG: 5576784
AME: 552832
BIM: 100742588
BTER: 100647936
SOC: 105193482
AEC: 105154304
ACEP: 105618894
PBAR: 105430839
HST: 105191076
CFO: 105256576
LHU: 105675201
PGC: 109860071
NVI: 100121709(Gnmt) 100122726
DPA: 109541622
NVL: 108569224
PMAC: 106708644
PRAP: 110995024
PXY: 105387574
ZNE: 110837685
FCD: 110843745
LAK: 106167602
EPA: 110240485
HMG: 100206590
 » show all
Taxonomy
Reference
1  [PMID:13971907]
  Authors
BLUMENSTEIN J, WILLIAMS GR.
  Title
Glycine methyltransferase.
  Journal
Can J Biochem Physiol 41:201-10 (1963)
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 30:13-26 (1998)
DOI:10.1016/S1357-2725(97)00105-2
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 274:37559-64 (1999)
DOI:10.1074/jbc.274.53.37559
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 204:521-32 (2000)
DOI:10.1006/jtbi.2000.2035
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 42:8394-402 (2003)
DOI:10.1021/bi034245a
  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 57:331-7 (2004)
DOI:10.1002/prot.20209
  Sequence
[hsa:27232] [mmu:14711]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.20
IUBMB Enzyme Nomenclature: 2.1.1.20
ExPASy - ENZYME nomenclature database: 2.1.1.20
BRENDA, the Enzyme Database: 2.1.1.20
CAS: 37228-72-1

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