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- guanidinoacetate methyltransferase
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/30 06:17:05」(JST)
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| Guanidinoacetate N-methyltransferase |
PDB rendering based on 1khh. |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
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3ORH
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| Identifiers |
| Symbols |
GAMT; PIG2; TP53I2 |
| External IDs |
OMIM: 601240 MGI: 1098221 HomoloGene: 32089 GeneCards: GAMT Gene |
| EC number |
2.1.1.2 |
| Gene Ontology |
| Molecular function |
• methyltransferase activity
• guanidinoacetate N-methyltransferase activity
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| Cellular component |
• cytosol
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| Biological process |
• creatine metabolic process
• creatine biosynthetic process
• muscle contraction
• spermatogenesis
• organ morphogenesis
• cellular nitrogen compound metabolic process
• regulation of multicellular organism growth
• small molecule metabolic process
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| Sources: Amigo / QuickGO |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
2593 |
14431 |
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| Ensembl |
ENSG00000130005 |
ENSMUSG00000020150 |
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| UniProt |
Q14353 |
O35969 |
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| RefSeq (mRNA) |
NM_000156 |
NM_010255 |
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| RefSeq (protein) |
NP_000147 |
NP_034385 |
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| Location (UCSC) |
Chr 19:
1.4 – 1.4 Mb |
Chr 10:
80.26 – 80.26 Mb |
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| PubMed search |
[1] |
[2] |
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| guanidinoacetate N-methyltransferase |
| Identifiers |
| EC number |
2.1.1.2 |
| CAS number |
9029-75-8 |
| 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 |
proteins |
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Guanidinoacetate N-methyltransferase (EC 2.1.1.2) is an enzyme that catalyzes the chemical reaction and is encoded by gene GAMT located on chromosome 19p13.3.[1]
- S-adenosyl-L-methionine + guanidinoacetate S-adenosyl-L-homocysteine + creatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and guanidinoacetate, whereas its two products are S-adenosylhomocysteine and creatine.
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:N-guanidinoacetate methyltransferase. Other names in common use include GA methylpherase, guanidinoacetate methyltransferase, guanidinoacetate transmethylase, methionine-guanidinoacetic transmethylase, and guanidoacetate methyltransferase. This enzyme participates in glycine, serine and threonine metabolism and arginine and proline metabolism.
The protein encoded by this gene is a methyltransferase that converts guanidoacetate to creatine, using S-adenosylmethionine as the methyl donor. Defects in this gene have been implicated in neurologic syndromes and muscular hypotonia, probably due to creatine deficiency and accumulation of guanidinoacetate in the brain of affected individuals. Two transcript variants encoding different isoforms have been described for this gene.[1]
Structural studies[edit]
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1KHH, 1P1B, 1P1C, 1XCJ, 1XCL, 1ZX0, and 2BLN.
See also[edit]
- Guanidinoacetate methyltransferase deficiency
References[edit]
- ^ a b "Entrez Gene: GAMT guanidinoacetate N-methyltransferase".
- Almeida LS, Vilarinho L, Darmin PS et al. (2007). "A prevalent pathogenic GAMT mutation (c.59G>C) in Portugal". Mol. Genet. Metab. 91 (1): 1–6. doi:10.1016/j.ymgme.2007.01.005. PMID 17336114.
- Morris AA, Appleton RE, Power B et al. (2007). "Guanidinoacetate methyltransferase deficiency masquerading as a mitochondrial encephalopathy". J. Inherit. Metab. Dis. 30 (1): 100–100. doi:10.1007/s10545-006-0478-2. PMID 17171576.
- Almeida LS, Rosenberg EH, Martinez-Muñoz C et al. (2007). "Overexpression of GAMT restores GAMT activity in primary GAMT-deficient fibroblasts". Mol. Genet. Metab. 89 (4): 392–4. doi:10.1016/j.ymgme.2006.06.006. PMID 16899382.
- Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Grimwood J, Gordon LA, Olsen A et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Komoto J, Huang Y, Hu Y et al. (2000). "Crystallization and preliminary x-ray diffraction studies of guanidinoacetate methyltransferase from rat liver". Acta Crystallogr. D Biol. Crystallogr. 55 (Pt 11): 1928–9. doi:10.1107/S0907444999010318. PMID 10531498.
- Chae YJ, Chung CE, Kim BJ et al. (1998). "The gene encoding guanidinoacetate methyltransferase (GAMT) maps to human chromosome 19 at band p13.3 and to mouse chromosome 10". Genomics 49 (1): 162–4. doi:10.1006/geno.1998.5236. PMID 9570966.
- Jenne DE, Olsen AS, Zimmer M (1997). "The human guanidinoacetate methyltransferase (GAMT) gene maps to a syntenic region on 19p13.3, homologous to band C of mouse chromosome 10, but GAMT is not mutated in jittery mice". Biochem. Biophys. Res. Commun. 238 (3): 723–7. doi:10.1006/bbrc.1997.9992. PMID 9325156.
- Polyak K, Xia Y, Zweier JL et al. (1997). "A model for p53-induced apoptosis". Nature 389 (6648): 300–5. doi:10.1038/38525. PMID 9305847.
- Stöckler S, Isbrandt D, Hanefeld F et al. (1996). "Guanidinoacetate methyltransferase deficiency: the first inborn error of creatine metabolism in man". Am. J. Hum. Genet. 58 (5): 914–22. PMC 1914613. PMID 8651275.
- Isbrandt D, von Figura K (1996). "Cloning and sequence analysis of human guanidinoacetate N-methyltransferase cDNA". Biochim. Biophys. Acta 1264 (3): 265–7. PMID 8547310.
- Cantoni GL and Scarano E (1954). "The formation of S-adenosylhomocysteine in enzymatic transmethylation reactions". J. Am. Chem. Soc. 76 (18): 4744. doi:10.1021/ja01647a081.
- CANTONI GL, VIGNOS PJ Jr (1954). "Enzymatic mechanism of creatine synthesis". J. Biol. Chem. 209 (2): 647–59. PMID 13192118.
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PDB gallery
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1khh: Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Template Structure of Protein Arginine Methyltransferase
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1p1b: Guanidinoacetate methyltransferase
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1p1c: Guanidinoacetate Methyltransferase with Gd ion
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1zx0: Human guanidinoacetate N-methyltransferase with SAH
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UpToDate Contents
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English Journal
- Creatine biosynthesis and transport in health and disease.
- Joncquel-Chevalier Curt M1, Voicu PM2, Fontaine M1, Dessein AF3, Porchet N1, Mention-Mulliez K4, Dobbelaere D4, Soto-Ares G5, Cheillan D6, Vamecq J7.
- Biochimie.Biochimie.2015 Nov 2. pii: S0300-9084(15)00342-9. doi: 10.1016/j.biochi.2015.10.022. [Epub ahead of print]
- Creatine is physiologically provided equally by diet and by endogenous synthesis from arginine and glycine with successive involvements of arginine glycine amidinotransferase [AGAT] and guanidinoacetate methyl transferase [GAMT]. A specific plasma membrane transporter, creatine transporter [CRTR] (S
- PMID 26542286
- Atorvastatin Increases miR-124a Expression: A Mechanism of Gamt Modulation in Liver Cells.
- Phulukdaree A1, Moodley D2, Khan S2, Chuturgoon AA2.
- Journal of cellular biochemistry.J Cell Biochem.2015 Nov;116(11):2620-7. doi: 10.1002/jcb.25209.
- Atorvastatin is used to control cholesterol and lipid levels in hyperlipidaemic and hypercholesterolaemic patients. Myopathy and hepatotoxicity, however, have been reported as side effects in a small percentage of statin users. This study aimed to investigate the cytotoxicity and the effect of atorv
- PMID 25926069
- Biosynthesis of homoarginine (hArg) and asymmetric dimethylarginine (ADMA) from acutely and chronically administered free L-arginine in humans.
- Kayacelebi AA1, Langen J, Weigt-Usinger K, Chobanyan-Jürgens K, Mariotti F, Schneider JY, Rothmann S, Frölich JC, Atzler D, Choe CU, Schwedhelm E, Huneau JF, Lücke T, Tsikas D.
- Amino acids.Amino Acids.2015 Sep;47(9):1893-908. doi: 10.1007/s00726-015-2012-3. Epub 2015 Jun 2.
- Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide (NO) synthesis, whereas L-arginine (Arg) and L-homoarginine (hArg) serve as substrates for NO synthesis. ADMA and other methylated arginines are generally believed to exclusively derive from guanidine (N (G))-methylated ar
- PMID 26031828
Japanese Journal
- OP-282-5 新規標的遺伝子GAMTを介したp53の新たな腫瘍制御メカニズム(腫瘍基礎-16,一般口演,第110回日本外科学会定期学術集会)
- Guanidinoacetate methyltransferase deficiency (GAMT)
- Methylation of gibberellins by Arabidopsis GAMT1 and GAMT2
Related Links
- gamt bietet neben dem eigenen Kursangebot auch Kurse im Namen anderer Veranstalter an. Die Anmeldung und Verwaltung der hier aufgeführten Kurse läuft über das gamt-Sekretariat.
- The official name of this gene is “guanidinoacetate N-methyltransferase.” GAMT is the gene's official symbol. The GAMT gene is also known by other names, listed below. Read more about gene names and symbols on ...
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