グリシン-N-メチル基転移酵素、グリシン-N-メチルトランスフェラーゼ、グリシンN-メチルトランスフェラーゼ
WordNet
- the 14th letter of the Roman alphabet (同)n
- the simplest amino acid found in proteins and the principal amino acid in sugar cane
- genus of Asiatic erect or sprawling herbs: soya bean (同)genus Glycine
PrepTutorEJDIC
- nitrogenの化学記号
- neodymiumの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/01/25 20:32:07」(JST)
[Wiki en表示]
glycine N-methyltransferase |
Identifiers |
EC number |
2.1.1.20 |
CAS number |
37228-72-1 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / EGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI Protein |
search |
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In enzymology, a glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + glycine S-adenosyl-L-homocysteine + sarcosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and glycine, whereas its two products are S-adenosylhomocysteine and sarcosine.
This enzyme belongs to the family of transferases, 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 structures have been solved for this class of enzymes, with PDB accession codes 1BHJ, 1D2C, 1D2G, 1D2H, 1KIA, 1NBH, 1NBI, 1R74, 1XVA, 2AZT, 2IDJ, and 2IDK.
References
- BLUMENSTEIN J, WILLIAMS GR (1963). "Glycine methyltransferase". Can. J. Biochem. Physiol. 41: 201–10. doi:10.1139/o63-025. PMID 13971907.
- Ogawa H, Gomi T, Takusagawa F, Fujioka M (1998). "Structure, function and physiological role of glycine N-methyltransferase". Int. J. Biochem. Cell. Biol. 30 (1): 13–26. doi:10.1016/S1357-2725(97)00105-2. PMID 9597750.
- Yeo EJ, Briggs WT, Wagner C (1999). "Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate". J. Biol. Chem. 274 (53): 37559–64. doi:10.1074/jbc.274.53.37559. PMID 10608809.
- FI; Vitvitsky, VM; Mosharov, EV; Banerjee, R; Ataullakhanov, FI (2000). "A substrate switch: a new mode of regulation in the methionine metabolic pathway". J. Theor. Biol. 204 (4): 521–32. doi:10.1006/jtbi.2000.2035. PMID 10833353.
- Fujioka M, Takusagawa F (2003). "Catalytic mechanism of glycine N-methyltransferase". Biochemistry. 42 (28): 8394–402. doi:10.1021/bi034245a. PMID 12859184.
- Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME (2004). "Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes". Proteins. 57 (2): 331–7. doi:10.1002/prot.20209. PMID 15340920.
UpToDate Contents
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English Journal
- PRMT1-mediated arginine methylation controls ATXN2L localization.
- Kaehler C1, Guenther A1, Uhlich A1, Krobitsch S2.
- Experimental cell research.Exp Cell Res.2015 May 15;334(1):114-25. doi: 10.1016/j.yexcr.2015.02.022. Epub 2015 Mar 5.
- Arginine methylation is a posttranslational modification that is of importance in diverse cellular processes. Recent proteomic mass spectrometry studies reported arginine methylation of ataxin-2-like (ATXN2L), the paralog of ataxin-2, a protein that is implicated in the neurodegenerative disorder sp
- PMID 25748791
- Expression of sarcosine metabolism-related proteins in invasive lobular carcinoma: comparison to invasive ductal carcinoma.
- Cha YJ1, Jung WH1, Cho NH1, Koo JS2.
- Yonsei medical journal.Yonsei Med J.2015 May;56(3):598-607. doi: 10.3349/ymj.2015.56.3.598.
- PURPOSE: The aims of this study were to compare the expression of sarcosine metabolism-related proteins between invasive lobular carcinoma (ILC) and invasive ductal carcinoma (IDC) and to determine the implications of these results.MATERIALS AND METHODS: Tissue microarrays were constructed, containi
- PMID 25837163
- Repression of the nuclear receptor small heterodimer partner by steatotic drugs and in advanced nonalcoholic fatty liver disease.
- Benet M1, Guzmán C1, Pisonero-Vaquero S1, García-Mediavilla MV1, Sánchez-Campos S1, Martínez-Chantar ML1, Donato MT1, Castell JV1, Jover R2.
- Molecular pharmacology.Mol Pharmacol.2015 Apr;87(4):582-94. doi: 10.1124/mol.114.096313. Epub 2015 Jan 9.
- The small heterodimer partner (SHP) (NR0B2) is an atypical nuclear receptor that lacks a DNA-binding domain. It interacts with and inhibits many transcription factors, affecting key metabolic processes, including bile acid, cholesterol, fatty acid, and drug metabolism. Our aim was to determine the i
- PMID 25576488
Japanese Journal
- Regulation of Folate-Mediated One-Carbon Metabolism by Glycine N-Methyltransferase (GNMT) and Methylenetetrahydrofolate Reductase (MTHFR)
- Journal of Nutritional Science and Vitaminology 61(Supplement), S148-S150, 2015
- NAID 130005109888
- クレアチンの網膜移行性と生合成 (第26回 生体膜と薬物の相互作用シンポジウム 講演要旨集)
- Glycine N-methyltransferase deficiency : A new patient with a novel mutation
Related Links
- In enzymology, a glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + glycine S-adenosyl-L-homocysteine + sarcosine Thus, the two substrates of this enzyme are S-adenosyl methionine ...
- Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue ...
★リンクテーブル★
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- 英
- glycine N-methyltransferase
- 関
- グリシン-N-メチルトランスフェラーゼ
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- 英
- glycine N-methyltransferase
- 関
- グリシン-N-メチル基転移酵素
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- 英
- glycine N-methyltransferase
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- 関
- number of experiment、sample size
- pの前の[n]はmと記載する。synptom→symptom
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メチルトランスフェラーゼ、メチル基転移酵素、メチル化酵素
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メチルトランスフェラーゼ
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ネオジム neodymium