AGXT

Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)
PDB rendering based on 1h0c.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1h0c​, 1j04​
Identifiers
Symbols	AGXT ; AGT; AGT1; AGXT1; PH1; SPAT; SPT; TLH6
External IDs	Template:OMIM5 Template:MGI HomoloGene: 37251
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase), also known as AGXT, is a human gene.

This gene is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria.

Further reading

• Danpure CJ (1993). "Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase". Biochimie. 75 (3–4): 309–15. PMID 8507692.
• Danpure CJ (2005). "Molecular etiology of primary hyperoxaluria type 1: new directions for treatment". Am. J. Nephrol. 25 (3): 303–10. doi:10.1159/000086362. PMID 15961951.
• Minatogawa Y, Tone S, Allsop J; et al. (1993). "A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1". Hum. Mol. Genet. 1 (8): 643–4. PMID 1301173.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Purdue PE, Lumb MJ, Allsop J; et al. (1992). "A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1". Genomics. 13 (1): 215–8. PMID 1349575.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Purdue PE, Takada Y, Danpure CJ (1991). "Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1". J. Cell Biol. 111 (6 Pt 1): 2341–51. PMID 1703535.CS1 maint: Multiple names: authors list (link)
• Purdue PE, Allsop J, Isaya G; et al. (1992). "Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation". Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10900–4. PMID 1961759.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nishiyama K, Funai T, Katafuchi R; et al. (1991). "Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene". Biochem. Biophys. Res. Commun. 176 (3): 1093–9. PMID 2039493.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Purdue PE, Lumb MJ, Fox M; et al. (1991). "Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase". Genomics. 10 (1): 34–42. PMID 2045108.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nishiyama K, Berstein G, Oda T, Ichiyama A (1991). "Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase". Eur. J. Biochem. 194 (1): 9–18. PMID 2253628.CS1 maint: Multiple names: authors list (link)
• Takada Y, Kaneko N, Esumi H; et al. (1990). "Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon". Biochem. J. 268 (2): 517–20. PMID 2363689.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Danpure CJ, Jennings PR (1986). "Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I.". FEBS Lett. 201 (1): 20–4. PMID 3709805.
• Danpure CJ, Fryer P, Jennings PR; et al. (1995). "Evolution of alanine:glyoxylate aminotransferase 1 peroxisomal and mitochondrial targeting. A survey of its subcellular distribution in the livers of various representatives of the classes Mammalia, Aves and Amphibia". Eur. J. Cell Biol. 64 (2): 295–313. PMID 7813517.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Danpure CJ, Purdue PE, Fryer P; et al. (1993). "Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation". Am. J. Hum. Genet. 53 (2): 417–32. PMID 8101040.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Minatogawa Y, Kawai C, Hatada S, Sato M (1997). "Liver specific kynurenine(alanine):glyoxylate aminotransferase was expressed in kidney cell line". Adv. Exp. Med. Biol. 398: 471–6. PMID 8906307.CS1 maint: Multiple names: authors list (link)
• von Schnakenburg C, Rumsby G (1997). "Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene". J. Med. Genet. 34 (6): 489–92. PMID 9192270.
• Amoroso A, Pirulli D, Puzzer D; et al. (1999). "Gene symbol: AGXT. Disease: primary hyperoxaluria type I.". Hum. Genet. 104 (5): 441. PMID 10394939.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pirulli D, Puzzer D, Ferri L; et al. (1999). "Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene". Hum. Genet. 104 (6): 523–5. PMID 10453743.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Basmaison O, Rolland MO, Cochat P, Bozon D (2000). "Identification of 5 novel mutations in the AGXT gene". Hum. Mutat. 15 (6): 577. doi:10.1002/1098-1004(200006)15:6<577::AID-HUMU9>3.0.CO;2-#. PMID 10862087.CS1 maint: Multiple names: authors list (link)
• Lumb MJ, Danpure CJ (2000). "Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations". J. Biol. Chem. 275 (46): 36415–22. doi:10.1074/jbc.M006693200. PMID 10960483.