GATM (gene): Difference between revisions
Jump to navigation
Jump to search
m Bot: HTTP→HTTPS |
removed underlinked template, added links from condition, condition grouping page, omim list of disorders and creatine |
||
| Line 1: | Line 1: | ||
{{Infobox_gene}} | {{Infobox_gene}} | ||
'''[[Glycine amidinotransferase]], [[mitochondrial]]''' is an [[enzyme]] that in humans is encoded by the ''GATM'' [[gene]].<ref name="pmid8313955">{{cite journal |vauthors=Humm A, Huber R, Mann K | title = The amino acid sequences of human and pig L-arginine:glycine amidinotransferase | journal = FEBS Lett | volume = 339 | issue = 1–2 | pages = 101–7 |date=Mar 1994 | pmid = 8313955 | pmc = | doi =10.1016/0014-5793(94)80394-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GATM glycine amidinotransferase (L-arginine:glycine amidinotransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2628| accessdate = }}</ref> | '''[[Glycine amidinotransferase]], [[mitochondrial]]''' is an [[enzyme]] that in humans is encoded by the ''GATM'' [[gene]].<ref name="pmid8313955">{{cite journal |vauthors=Humm A, Huber R, Mann K | title = The amino acid sequences of human and pig L-arginine:glycine amidinotransferase | journal = FEBS Lett | volume = 339 | issue = 1–2 | pages = 101–7 |date=Mar 1994 | pmid = 8313955 | pmc = | doi =10.1016/0014-5793(94)80394-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GATM glycine amidinotransferase (L-arginine:glycine amidinotransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2628| accessdate = }}</ref> | ||
| Line 6: | Line 5: | ||
{{PBB_Summary | {{PBB_Summary | ||
| section_title = | | section_title = | ||
| summary_text = This gene encodes a mitochondrial enzyme that belongs to the Amidinotransferase family. This enzyme is involved in [[creatine]] [[biosynthesis]], whereby it catalyzes the transfer of a guanido group from [[L-arginine]] to [[glycine]], resulting in guanidinoacetic acid, the immediate precursor of creatine. [[Mutations]] in this gene cause [[arginine | | summary_text = This gene encodes a mitochondrial enzyme that belongs to the Amidinotransferase family. This enzyme is involved in [[creatine]] [[biosynthesis]], whereby it catalyzes the transfer of a guanido group from [[L-arginine]] to [[glycine]], resulting in guanidinoacetic acid, the immediate precursor of creatine. [[Mutations]] in this gene cause [[arginine:glycine amidinotransferase deficiency]], an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.<ref name="entrez" /> | ||
}} | }} | ||
| Line 23: | Line 22: | ||
*{{cite journal |vauthors=Humm A, Fritsche E, Steinbacher S, Huber R |title=Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis |journal=EMBO J. |volume=16 |issue= 12 |pages= 3373–85 |year= 1997 |pmid= 9218780 |doi= 10.1093/emboj/16.12.3373 | pmc=1169963 }} | *{{cite journal |vauthors=Humm A, Fritsche E, Steinbacher S, Huber R |title=Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis |journal=EMBO J. |volume=16 |issue= 12 |pages= 3373–85 |year= 1997 |pmid= 9218780 |doi= 10.1093/emboj/16.12.3373 | pmc=1169963 }} | ||
*{{cite journal |vauthors=Fritsche E, Humm A, Huber R |title=Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study |journal=Eur. J. Biochem. |volume=247 |issue= 2 |pages= 483–90 |year= 1997 |pmid= 9266688 |doi=10.1111/j.1432-1033.1997.00483.x }} | *{{cite journal |vauthors=Fritsche E, Humm A, Huber R |title=Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study |journal=Eur. J. Biochem. |volume=247 |issue= 2 |pages= 483–90 |year= 1997 |pmid= 9266688 |doi=10.1111/j.1432-1033.1997.00483.x }} | ||
*{{cite journal | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 | author2= | *{{cite journal | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 | author2=Yoshirtomo-Nakagawa K | author3=Maruyama K | display-authors=3 | last4=Suyama | first4=A | last5=Sugano | first5=S }} | ||
*{{cite journal |vauthors=Fritsche E, Humm A, Huber R |title=The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 3026–32 |year= 1999 |pmid= 9915841 |doi=10.1074/jbc.274.5.3026 }} | *{{cite journal |vauthors=Fritsche E, Humm A, Huber R |title=The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 3026–32 |year= 1999 |pmid= 9915841 |doi=10.1074/jbc.274.5.3026 }} | ||
*{{cite journal | author=Item CB |title=Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans |journal=Am. J. Hum. Genet. |volume=69 |issue= 5 |pages= 1127–33 |year= 2001 |pmid= 11555793 |doi=10.1086/323765 | pmc=1274356 | author2=Stöckler-Ipsiroglu S | author3=Stromberger C | display-authors=3 | last4=Muhl | first4=A | last5=Alessandri | first5=M | last6=Bianchi | first6=M | last7=Tosetti | first7=M | last8=Fornai | first8=F | last9=Cioni | first9=G }} | *{{cite journal | author=Item CB |title=Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans |journal=Am. J. Hum. Genet. |volume=69 |issue= 5 |pages= 1127–33 |year= 2001 |pmid= 11555793 |doi=10.1086/323765 | pmc=1274356 | author2=Stöckler-Ipsiroglu S | author3=Stromberger C | display-authors=3 | last4=Muhl | first4=A | last5=Alessandri | first5=M | last6=Bianchi | first6=M | last7=Tosetti | first7=M | last8=Fornai | first8=F | last9=Cioni | first9=G }} | ||
Revision as of 19:49, 26 September 2018
| VALUE_ERROR (nil) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Aliases | |||||||
| External IDs | GeneCards: [1] | ||||||
| Orthologs | |||||||
| Species | Human | Mouse | |||||
| Entrez |
|
| |||||
| Ensembl |
|
| |||||
| UniProt |
|
| |||||
| RefSeq (mRNA) |
|
| |||||
| RefSeq (protein) |
|
| |||||
| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
| Wikidata | |||||||
| |||||||
Glycine amidinotransferase, mitochondrial is an enzyme that in humans is encoded by the GATM gene.[1][2]
This gene encodes a mitochondrial enzyme that belongs to the Amidinotransferase family. This enzyme is involved in creatine biosynthesis, whereby it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine. Mutations in this gene cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.[2]
References
- ↑ Humm A, Huber R, Mann K (Mar 1994). "The amino acid sequences of human and pig L-arginine:glycine amidinotransferase". FEBS Lett. 339 (1–2): 101–7. doi:10.1016/0014-5793(94)80394-3. PMID 8313955.
- ↑ 2.0 2.1 "Entrez Gene: GATM glycine amidinotransferase (L-arginine:glycine amidinotransferase)".
Further reading
- Humm A, Fritsche E, Steinbacher S (1997). "Structure and reaction mechanism of L-arginine:glycine amidinotransferase". Biol. Chem. 378 (3–4): 193–7. doi:10.1515/bchm.1997.378.3-4.121. PMID 9165070.
- Schulze A (2003). "Creatine deficiency syndromes". Mol. Cell. Biochem. 244 (1–2): 143–50. doi:10.1023/A:1022443503883. PMID 12701824.
- Gross MD, Eggen MA, Simon AM, Van Pilsum JF (1987). "The purification and characterization of human kidney L-arginine:glycine amidinotransferase". Arch. Biochem. Biophys. 251 (2): 747–55. doi:10.1016/0003-9861(86)90385-1. PMID 3800397.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Humm A; Fritsche E; Mann K; et al. (1997). "Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue". Biochem. J. 322 (3): 771–6. PMC 1218254. PMID 9148748.
- Humm A, Fritsche E, Steinbacher S, Huber R (1997). "Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis". EMBO J. 16 (12): 3373–85. doi:10.1093/emboj/16.12.3373. PMC 1169963. PMID 9218780.
- Fritsche E, Humm A, Huber R (1997). "Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study". Eur. J. Biochem. 247 (2): 483–90. doi:10.1111/j.1432-1033.1997.00483.x. PMID 9266688.
- Suzuki Y; Yoshirtomo-Nakagawa K; Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Fritsche E, Humm A, Huber R (1999). "The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study". J. Biol. Chem. 274 (5): 3026–32. doi:10.1074/jbc.274.5.3026. PMID 9915841.
- Item CB; Stöckler-Ipsiroglu S; Stromberger C; et al. (2001). "Arginine:glycine amidinotransferase deficiency: the third inborn error of creatine metabolism in humans". Am. J. Hum. Genet. 69 (5): 1127–33. doi:10.1086/323765. PMC 1274356. PMID 11555793.
- Carducci C; Birarelli M; Leuzzi V; et al. (2002). "Guanidinoacetate and creatine plus creatinine assessment in physiologic fluids: an effective diagnostic tool for the biochemical diagnosis of arginine:glycine amidinotransferase and guanidinoacetate methyltransferase deficiencies". Clin. Chem. 48 (10): 1772–8. PMID 12324495.
- Battini R; Leuzzi V; Carducci C; et al. (2003). "Creatine depletion in a new case with AGAT deficiency: clinical and genetic study in a large pedigree". Mol. Genet. Metab. 77 (4): 326–31. doi:10.1016/S1096-7192(02)00175-0. PMID 12468279.
- 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.
- Verhoeven NM; Schor DS; Roos B; et al. (2003). "Diagnostic enzyme assay that uses stable-isotope-labeled substrates to detect L-arginine:glycine amidinotransferase deficiency". Clin. Chem. 49 (5): 803–5. doi:10.1373/49.5.803. PMID 12709373.
- Ota T; Suzuki Y; Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- 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.
- Alessandrì MG; Celati L; Battini R; et al. (2005). "Gas chromatography/mass spectrometry assay for arginine: glycine-amidinotransferase deficiency". Anal. Biochem. 343 (2): 356–8. doi:10.1016/j.ab.2005.05.003. PMID 15978539.
External links
 | This article on a gene on human chromosome 15 is a stub. You can help Wikipedia by expanding it. |