// Workers AI · dad joke modeWhat did AGXT gene say? "I'm ex-pressed

AGXT
Identifiers
Aliases	AGXT, AGT, AGT1, AGXT1, PH1, SPAT, SPT, TLH6, alanine-glyoxylate aminotransferase, alanine--glyoxylate and serine--pyruvate aminotransferase, Ser-PyrAT
External IDs	OMIM: 604285; MGI: 1329033; HomoloGene: 37251; GeneCards: AGXT; OMA:AGXT - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1H0C, 1J04, 2YOB, 3R9A, 4CBR, 4CBS, 4I8A, 4KXK, 4KYO
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 2.6.1.44 ↗ ↗ ↗ ↗ 2.6.1.51 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 2 (human) Band 2q37.3 Start 240,868,824 bp End 240,880,502 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 D|1 47.0 cM Start 93,062,962 bp End 93,073,143 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver buccal mucosa cell cartilage tissue human kidney testicle kidney tubule cerebellar vermis gonad renal medulla renal cortex Top expressed in left lobe of liver embryo gallbladder sexually immature organism gastrula duodenum jejunum Ileal epithelium CA3 field submandibular gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity protein homodimerization activity amino acid binding alanine-glyoxylate transaminase activity serine-pyruvate transaminase activity transaminase activity protein self-association catalytic activity protein binding pyridoxal phosphate binding signaling receptor binding identical protein binding Cellular component peroxisome mitochondrial matrix peroxisomal matrix mitochondrion intracellular membrane-bounded organelle cytosol Biological process Notch signaling pathway oxalic acid secretion glyoxylate catabolic process glycine biosynthetic process, by transamination of glyoxylate pyruvate biosynthetic process L-alanine catabolic process response to glucocorticoid response to cAMP L-cysteine catabolic process cellular nitrogen compound metabolic process glyoxylate metabolic process protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 189 11611 Ensembl ENSG00000172482 ENSMUSG00000026272 UniProt P21549 O35423 RefSeq (mRNA) NM_000030 NM_001276710 NM_016702 RefSeq (protein) NP_000021 NP_001263639 NP_057911 Location (UCSC) Chr 2: 240.87 – 240.88 Mb Chr 1: 93.06 – 93.07 Mb PubMed search
Wikidata
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Serine—pyruvate aminotransferase is an enzyme that in humans is encoded by the AGXT 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 targeting, have been associated with type I primary hyperoxaluria.

See also

• Peroxisomal disorder

External links

• GeneReviews/NIH/NCBI/UW entry on Primary Hyperoxaluria Type 1
• Human AGT genome location and AGT gene details page in the UCSC Genome Browser.
• Human AGXT genome location and AGXT gene details page in the UCSC Genome Browser.

Further reading

• Danpure CJ (1993). "Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase". Biochimie. 75 (3–4): 309–15. doi:10.1016/0300-9084(93)90091-6. 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. doi:10.1093/hmg/1.8.643. PMID 1301173.
• 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. doi:10.1016/0888-7543(92)90225-H. PMID 1349575.
• 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. doi:10.1083/jcb.111.6.2341. PMC 2116406. PMID 1703535.
• 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. doi:10.1073/pnas.88.23.10900. PMC 53039. PMID 1961759.
• 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. doi:10.1111/j.1432-1033.1990.tb19420.x. hdl:10271/960. PMID 2253628. S2CID 953132.
• 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. doi:10.1042/bj2680517. PMC 1131464. PMID 2363689.
• Danpure CJ, Jennings PR (1986). "Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I". FEBS Lett. 201 (1): 20–4. doi:10.1016/0014-5793(86)80563-4. PMID 3709805. S2CID 32933133.
• 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.
• 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. PMC 1682352. PMID 8101040.
• Minatogawa Y, Kawai C, Hatada S, Sato M (1996). "Liver Specific Kynurenine (Alanine)". Recent Advances in Tryptophan Research. Adv. Exp. Med. Biol. Vol. 398. pp. 471–6. doi:10.1007/978-1-4613-0381-7_73. ISBN 978-1-4613-8026-9. PMID 8906307.
• 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. doi:10.1136/jmg.34.6.489. PMC 1050973. PMID 9192270.
• Amoroso A, Pirulli D, Puzzer D, et al. (1999). "Gene symbol: AGXT. Disease: primary hyperoxaluria type I". Hum. Genet. 104 (5): 441. doi:10.1007/s004390050984. PMID 10394939. S2CID 34307977.
• 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. doi:10.1007/s004390050998. PMID 10453743. S2CID 28076033.
• 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. S2CID 196606396.
• 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.