GATM (gene)

GATM
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1JDW, 1JDX, 2JDW, 2JDX, 3JDW, 4JDW, 5JDW, 6JDW, 7JDW, 8JDW, 9JDW
Identifiers
Aliases	GATM , AGAT, AT, CCDS3, glycine amidinotransferase, FRTS1
External IDs	OMIM: 602360; MGI: 1914342; HomoloGene: 1136; GeneCards: GATM; OMA:GATM - orthologs
Gene location (Human) Chr. Chromosome 15 (human) [1] Band 15q21.1 Start 45,361,124 bp [1] End 45,402,327 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 E5|2 60.63 cM Start 122,424,948 bp [2] End 122,441,784 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas right lobe of liver jejunal mucosa corpus callosum renal medulla kidney tubule trigeminal ganglion olfactory bulb spinal cord human kidney Top expressed in right kidney human kidney thoracic diaphragm primary visual cortex striatum of neuraxis hippocampus proper pancreas cerebellar cortex superior frontal gyrus olfactory bulb More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity glycine amidinotransferase activity amidinotransferase activity Cellular component membrane cytoplasm mitochondrial inner membrane extracellular exosome mitochondrial intermembrane space mitochondrion Biological process creatine biosynthetic process creatine metabolic process multicellular organism development learning or memory muscle atrophy positive regulation of cold-induced thermogenesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2628 67092 Ensembl ENSG00000171766 ENSMUSG00000027199 UniProt P50440 Q9D964 RefSeq (mRNA) NM_001482 NM_001321015 NM_025961 RefSeq (protein) NP_001307944 NP_001473 NP_080237 Location (UCSC) Chr 15: 45.36 – 45.4 Mb Chr 2: 122.42 – 122.44 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glycine amidinotransferase, mitochondrial is an enzyme that in humans is encoded by the GATM gene. ^{[5] [6]}

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. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000171766 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027199 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. Bibcode:1994FEBSL.339..101H. doi:10.1016/0014-5793(94)80394-3. PMID   8313955. S2CID   41884725.
6. "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. S2CID   25056424.
• 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. doi:10.1042/bj3220771. 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. doi: 10.1093/clinchem/48.10.1772 . 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. Bibcode:2002PNAS...9916899M. 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

• GeneReviews/NCBI/NIH/UW entry on Creatine Deficiency Syndromes