Mammalian protein found in Homo sapiens
GAMT |
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![](//upload.wikimedia.org/wikipedia/commons/thumb/f/ff/Protein_GAMT_PDB_1khh.png/250px-Protein_GAMT_PDB_1khh.png) |
Available structures |
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PDB | Ortholog search: PDBe RCSB |
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Identifiers |
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Aliases | GAMT, CCDS2, HEL-S-20, PIG2, TP53I2, guanidinoacetate N-methyltransferase |
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External IDs | OMIM: 601240; MGI: 1098221; HomoloGene: 32089; GeneCards: GAMT; OMA:GAMT - orthologs |
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Gene location (Human) |
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![Chromosome 19 (human)](//upload.wikimedia.org/wikipedia/commons/thumb/5/54/Ideogram_human_chromosome_19.svg/300px-Ideogram_human_chromosome_19.svg.png) | Chr. | Chromosome 19 (human)[1] |
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| Band | 19p13.3 | Start | 1,397,026 bp[1] |
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End | 1,401,570 bp[1] |
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Gene location (Mouse) |
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![Chromosome 10 (mouse)](//upload.wikimedia.org/wikipedia/commons/thumb/4/4e/Ideogram_house_mouse_chromosome_10.svg/260px-Ideogram_house_mouse_chromosome_10.svg.png) | Chr. | Chromosome 10 (mouse)[2] |
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| Band | 10 C1|10 39.72 cM | Start | 80,093,985 bp[2] |
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End | 80,096,846 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - muscle of thigh
- right lobe of liver
- gastrocnemius muscle
- Skeletal muscle tissue of rectus abdominis
- triceps brachii muscle
- vastus lateralis muscle
- glutes
- thoracic diaphragm
- biceps brachii
- Skeletal muscle tissue of biceps brachii
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| Top expressed in | - left lobe of liver
- adrenal gland
- yolk sac
- gallbladder
- right kidney
- muscle of thigh
- esophagus
- triceps brachii muscle
- proximal tubule
- temporal muscle
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| More reference expression data |
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BioGPS | ![](//upload.wikimedia.org/wikipedia/commons/thumb/d/dd/PBB_GE_GAMT_205354_at_fs.png/250px-PBB_GE_GAMT_205354_at_fs.png) | More reference expression data |
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Gene ontology |
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Molecular function | - methyltransferase activity
- transferase activity
- guanidinoacetate N-methyltransferase activity
- S-adenosylmethionine-dependent methyltransferase activity
| Cellular component | - cytoplasm
- cytosol
- nucleus
| Biological process | - muscle contraction
- regulation of multicellular organism growth
- methylation
- spermatogenesis
- animal organ morphogenesis
- creatine metabolic process
- creatine biosynthetic process
- S-adenosylhomocysteine metabolic process
- S-adenosylmethionine metabolic process
| Sources:Amigo / QuickGO |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | | |
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Location (UCSC) | Chr 19: 1.4 – 1.4 Mb | Chr 10: 80.09 – 80.1 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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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.[5]
- 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.[5]
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
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000130005 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020150 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: GAMT guanidinoacetate N-methyltransferase".
Further reading
- 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. doi:10.1007/s10545-006-0478-2. PMID 17171576. S2CID 20768084.
- 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. Bibcode:2004Natur.428..529G. 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. Bibcode:2002PNAS...9916899M. 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" (PDF). Acta Crystallogr. D. 55 (Pt 11): 1928–9. doi:10.1107/S0907444999010318. hdl:1808/17175. 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. Bibcode:1997Natur.389..300P. doi:10.1038/38525. PMID 9305847. S2CID 4429638.
- 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, 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 (1954). "Enzymatic mechanism of creatine synthesis". J. Biol. Chem. 209 (2): 647–59. doi:10.1016/S0021-9258(18)65492-4. PMID 13192118.
External links
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Guanidinoacetate N-methyltransferase
PDB gallery
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1khh: Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Template Structure of Protein Arginine Methyltransferase -
1p1b: Guanidinoacetate methyltransferase -
1p1c: Guanidinoacetate Methyltransferase with Gd ion -
1zx0: Human guanidinoacetate N-methyltransferase with SAH |
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