グアニジノ・酸-N-メチルトランスフェラーゼ
WordNet
- the 14th letter of the Roman alphabet (同)n
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）』「2015/07/29 13:53:06」(JST)
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| Guanidinoacetate N-methyltransferase |
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PDB rendering based on 1khh.
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| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
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3ORH
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| Identifiers |
| Symbols |
GAMT ; CCDS2; HEL-S-20; 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
• protein homodimerization activity
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| Cellular component |
• cytosol
• extracellular exosome
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| Biological process |
• creatine metabolic process
• creatine biosynthetic process
• muscle contraction
• spermatogenesis
• organ morphogenesis
• methylation
• cellular nitrogen compound metabolic process
• regulation of multicellular organism growth
• small molecule metabolic process
• S-adenosylhomocysteine metabolic process
• S-adenosylmethionine metabolic process
• embryonic liver development
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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 |
| Entrez |
2593 |
14431 |
| Ensembl |
ENSG00000130005 |
ENSMUSG00000020150 |
| UniProt |
Q14353 |
O35969 |
| RefSeq (mRNA) |
NM_000156 |
NM_010255 |
| RefSeq (protein) |
NP_000147 |
NP_034385 |
| Location (UCSC) |
Chr 19:
1.4 – 1.4 Mb |
Chr 10:
80.26 – 80.26 Mb |
| 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
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
- Guanidinoacetate methyltransferase deficiency
References
- ^ 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. doi:10.1016/0167-4781(95)00184-0. 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
- Increased methylation demand exacerbates ethanol-induced liver injury.
- Kharbanda KK1, Todero SL2, Thomes PG3, Orlicky DJ4, Osna NA3, French SW5, Tuma DJ3.
- Experimental and molecular pathology.Exp Mol Pathol.2014 Aug;97(1):49-56. doi: 10.1016/j.yexmp.2014.05.006. Epub 2014 May 16.
- We previously reported that chronic ethanol intake lowers hepatocellular S-adenosylmethionine to S-adenosylhomocysteine ratio and significantly impairs many liver methylation reactions. One such reaction, catalyzed by guanidinoacetate methyltransferase (GAMT), is a major consumer of methyl groups an
- PMID 24842317
- Alcohol consumption decreases rat hepatic creatine biosynthesis via altered guanidinoacetate methyltransferase activity.
- Kharbanda KK1, Todero SL, Moats JC, Harris RM, Osna NA, Thomes PG, Tuma DJ.
- Alcoholism, clinical and experimental research.Alcohol Clin Exp Res.2014 Mar;38(3):641-8. doi: 10.1111/acer.12306. Epub 2013 Nov 20.
- BACKGROUND: We have previously shown that decreased S-adenosylmethionine (SAM):S-adenosylhomocysteine (SAH) ratio generated in livers of alcohol-fed rats can impair the activities of many SAM-dependent methyltransferases. One such methyltransferase is guanidinoacetate methyltransferase (GAMT) that c
- PMID 24256608
- Synthesis of guanidinoacetate and creatine from amino acids by rat pancreas.
- da Silva RP1, Clow K1, Brosnan JT1, Brosnan ME1.
- The British journal of nutrition.Br J Nutr.2014 Feb;111(4):571-7. doi: 10.1017/S0007114513003012. Epub 2013 Oct 8.
- Creatine is an important molecule involved in cellular energy metabolism. Creatine is spontaneously converted to creatinine at a rate of 1·7% per d; creatinine is lost in the urine. Creatine can be obtained from the diet or synthesised from endogenous amino acids via the enzymes arginine:glycine am
- PMID 24103317
Japanese Journal
- Cytochemical and cytological properties of perineuronal oligodendrocytes in the mouse cortex
- 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)
- Identification of 197 genetic variations in six human methyltransferase genes in the Japanese population
Related Links
- 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 ...
- cytoplasm, cytosol, extracellular exosome, nucleus, guanidinoacetate N-methyltransferase activity, methyltransferase activity, cellular nitrogen compound metabolic process, creatine biosynthetic process, creatine metabolic process ... ...
Related Pictures
★リンクテーブル★
[★]
- 英
- guanidinoacetate N-methyltransferase
[★]
- 関
- number of experiment、sample size
- pの前の[n]はmと記載する。synptom→symptom
[★]
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
[★]
[★]
メチルトランスフェラーゼ
[★]
ネオジム neodymium