Guanidinoacetate N-methyltransferase: Difference between revisions

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{{PBB|geneid=2593}}
{{enzyme
{{enzyme
| Name = guanidinoacetate N-methyltransferase
| Name = guanidinoacetate N-methyltransferase
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{{Mergeto|GAMT|date=May 2008}}
In [[enzymology]], a '''guanidinoacetate N-methyltransferase''' ({{EC number|2.1.1.2}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
'''Guanidinoacetate N-methyltransferase''' ({{EC number|2.1.1.2}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] and is encoded by gene ''GAMT'' located on chromosome 19p13.3.<ref name="entrez">{{cite web | title = Entrez Gene: GAMT guanidinoacetate N-methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2593| accessdate = }}</ref>


:S-adenosyl-L-methionine + guanidinoacetate <math>\rightleftharpoons</math> S-adenosyl-L-homocysteine + creatine
:S-adenosyl-L-methionine + guanidinoacetate <math>\rightleftharpoons</math> S-adenosyl-L-homocysteine + creatine
Line 17: Line 18:


This enzyme belongs to the family of [[transferase]]s, 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]].
This enzyme belongs to the family of [[transferase]]s, 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.<ref name="entrez" />


==Structural studies==
==Structural studies==


As of late 2007, 7 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1KHH}}, {{PDB link|1P1B}}, {{PDB link|1P1C}}, {{PDB link|1XCJ}}, {{PDB link|1XCL}}, {{PDB link|1ZX0}}, and {{PDB link|2BLN}}.
As of late 2007, 7 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1KHH}}, {{PDB link|1P1B}}, {{PDB link|1P1C}}, {{PDB link|1XCJ}}, {{PDB link|1XCL}}, {{PDB link|1ZX0}}, and {{PDB link|2BLN}}.

==See also==
* [[Guanidinoacetate methyltransferase deficiency]]


==References==
==References==
{{reflist|1}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Almeida LS |title=A prevalent pathogenic GAMT mutation (c.59G>C) in Portugal |journal=Mol. Genet. Metab. |volume=91 |issue= 1 |pages= 1–6 |year= 2007 |pmid= 17336114 |doi= 10.1016/j.ymgme.2007.01.005 | author-separator=, | author2=Vilarinho L | author3=Darmin PS | display-authors=3 | last4=Rosenberg | first4=E.H. | last5=Martinez-Muñoz | first5=C. | last6=Jakobs | first6=C. | last7=Salomons | first7=G.S. }}
*{{cite journal | author=Morris AA |title=Guanidinoacetate methyltransferase deficiency masquerading as a mitochondrial encephalopathy |journal=J. Inherit. Metab. Dis. |volume=30 |issue= 1 |pages= 100–100 |year= 2007 |pmid= 17171576 |doi= 10.1007/s10545-006-0478-2 | author-separator=, | author2=Appleton RE | author3=Power B | display-authors=3 | last4=Isherwood | first4=D. M. | last5=Abernethy | first5=L. J. | last6=Taylor | first6=R. W. | last7=Turnbull | first7=D. M. | last8=Verhoeven | first8=N. M. | last9=Salomons | first9=G. S. }}
*{{cite journal | author=Almeida LS |title=Overexpression of GAMT restores GAMT activity in primary GAMT-deficient fibroblasts |journal=Mol. Genet. Metab. |volume=89 |issue= 4 |pages= 392–4 |year= 2007 |pmid= 16899382 |doi= 10.1016/j.ymgme.2006.06.006 | author-separator=, | author2=Rosenberg EH | author3=Martinez-Muñoz C | display-authors=3 | last4=Verhoeven | first4=N.M. | last5=Vilarinho | first5=L. | last6=Jakobs | first6=C. | last7=Salomons | first7=G.S. }}
*{{cite journal | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 | author-separator=, | author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
*{{cite journal | author=Grimwood J |title=The DNA sequence and biology of human chromosome 19 |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 | author-separator=, | author2=Gordon LA | author3=Olsen A | display-authors=3 | last4=Terry | first4=Astrid | last5=Schmutz | first5=Jeremy | last6=Lamerdin | first6=Jane | last7=Hellsten | first7=Uffe | last8=Goodstein | first8=David | last9=Couronne | first9=Olivier }}
*{{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 | author-separator=, | author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }}
*{{cite journal | author=Komoto J |title=Crystallization and preliminary x-ray diffraction studies of guanidinoacetate methyltransferase from rat liver |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=55 |issue= Pt 11 |pages= 1928–9 |year= 2000 |pmid= 10531498 |doi=10.1107/S0907444999010318 | author-separator=, | author2=Huang Y | author3=Hu Y | display-authors=3 | last4=Takata | first4=Yoshimi | last5=Konishi | first5=Kiyoshi | last6=Ogawa | first6=Hirofumi | last7=Gomi | first7=Tomoharu | last8=Fujioka | first8=Motoji | last9=Takusagawa | first9=Fusao }}
*{{cite journal | author=Chae YJ |title=The gene encoding guanidinoacetate methyltransferase (GAMT) maps to human chromosome 19 at band p13.3 and to mouse chromosome 10 |journal=Genomics |volume=49 |issue= 1 |pages= 162–4 |year= 1998 |pmid= 9570966 |doi= 10.1006/geno.1998.5236 | author-separator=, | author2=Chung CE | author3=Kim BJ | display-authors=3 | last4=Lee | first4=MH | last5=Lee | first5=H }}
*{{cite journal | author=Jenne DE, Olsen AS, Zimmer M |title=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 |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 3 |pages= 723–7 |year= 1997 |pmid= 9325156 |doi= 10.1006/bbrc.1997.9992 }}
*{{cite journal | author=Polyak K |title=A model for p53-induced apoptosis |journal=Nature |volume=389 |issue= 6648 |pages= 300–5 |year= 1997 |pmid= 9305847 |doi= 10.1038/38525 | author-separator=, | author2=Xia Y | author3=Zweier JL | display-authors=3 | last4=Kinzler | first4=Kenneth W. | last5=Vogelstein | first5=Bert }}
*{{cite journal | author=Stöckler S |title=Guanidinoacetate methyltransferase deficiency: the first inborn error of creatine metabolism in man |journal=Am. J. Hum. Genet. |volume=58 |issue= 5 |pages= 914–22 |year= 1996 |pmid= 8651275 |doi= | pmc=1914613 | author-separator=, | author2=Isbrandt D | author3=Hanefeld F | display-authors=3 | last4=Schmidt | first4=B | last5=Von Figura | first5=K }}
*{{cite journal | author=Isbrandt D, von Figura K |title=Cloning and sequence analysis of human guanidinoacetate N-methyltransferase cDNA |journal=Biochim. Biophys. Acta |volume=1264 |issue= 3 |pages= 265–7 |year= 1996 |pmid= 8547310 |doi= }}
* {{cite journal | author = Cantoni GL and Scarano E | date = 1954 | title = The formation of S-adenosylhomocysteine in enzymatic transmethylation reactions | journal = J. Am. Chem. Soc. | volume = 76 | pages = 4744 | doi = 10.1021/ja01647a081 }}
* {{cite journal | author = Cantoni GL and Scarano E | date = 1954 | title = The formation of S-adenosylhomocysteine in enzymatic transmethylation reactions | journal = J. Am. Chem. Soc. | volume = 76 | pages = 4744 | doi = 10.1021/ja01647a081 }}
* {{cite journal | author = CANTONI GL, VIGNOS PJ Jr | date = 1954 | title = Enzymatic mechanism of creatine synthesis | journal = J. Biol. Chem. | volume = 209 | pages = 647&ndash;59 | pmid = 13192118 | issue = 2 }}
* {{cite journal | author = CANTONI GL, VIGNOS PJ Jr | date = 1954 | title = Enzymatic mechanism of creatine synthesis | journal = J. Biol. Chem. | volume = 209 | pages = 647&ndash;59 | pmid = 13192118 | issue = 2 }}
}}
{{refend}}




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[[Category:EC 2.1.1]]
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[[it:Guanidinoacetato N-metiltransferasi]]
[[it:Guanidinoacetato N-metiltransferasi]]
[[de:Guanidinoacetat-N-Methyltransferase]]
[[ja:グアニジノ酢酸-N-メチルトランスフェラーゼ]]
[[ja:グアニジノ酢酸-N-メチルトランスフェラーゼ]]

Revision as of 23:07, 23 June 2011

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guanidinoacetate N-methyltransferase
Identifiers
EC no.2.1.1.2
CAS no.9029-75-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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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

References

Template:PBB Further reading



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  1. ^ a b "Entrez Gene: GAMT guanidinoacetate N-methyltransferase".
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