AGXT

Alanine-glyoxylate aminotransferase

PDB rendering based on 1h0c.

Available structures
PDB	1H0C, 1J04, 3IMZ

Identifiers

Symbols

AGXT; AGT; AGT1; AGXT1; PH1; SPAT; SPT; TLH6

External IDs

OMIM: 604285 MGI: 1329033 HomoloGene: 37251 GeneCards: AGXT Gene

Gene Ontology
Molecular function	• serine-pyruvate transaminase activity • protein binding • alanine-glyoxylate transaminase activity • amino acid binding • transferase activity • pyridoxal phosphate binding • protein homodimerization activity
Cellular component	• mitochondrion • mitochondrial matrix • peroxisome • peroxisomal matrix
Biological process	• protein targeting to peroxisome • glycine biosynthetic process, by transamination of glyoxylate • cellular nitrogen compound metabolic process • pyruvate biosynthetic process • glyoxylate metabolic process • glyoxylate metabolic process • oxalic acid secretion • response to glucocorticoid stimulus • response to cAMP
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
241.81 – 241.82 Mb

Chr 1:
95.03 – 95.04 Mb

PubMed search

[1]

[2]

Serine—pyruvate aminotransferase is an enzyme that in humans is encoded by the AGXT gene.^[1]^[2]^[3]

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.^[3]

References

^ Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A (Jul 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. doi:10.1016/0006-291X(91)90396-O. PMID 2039493.
^ Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ (Jul 1991). "Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase". Genomics 10 (1): 34–42. doi:10.1016/0888-7543(91)90481-S. PMID 2045108.
^ ^a ^b "Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189.

External links

GeneReviews/NIH/NCBI/UW entry on Primary Hyperoxaluria Type 1

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2116406.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53039.
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. PMID 2253628.
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. PMC 1131464. PMID 2363689. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1131464.
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.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1682352.
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.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1050973.
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.
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.
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.
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.

PDB gallery

1h0c: THE CRYSTAL STRUCTURE OF HUMAN ALANINE:GLYOXYLATE AMINOTRANSFERASE

1j04: Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro

Transferase: nitrogenous groups (EC 2.6)

2.6.1: Transaminases	Aspartate transaminase (GOT1, GOT2) · Alanine transaminase · GABA transaminase · Tyrosine aminotransferase · Ornithine aminotransferase · Branched chain aminotransferase · Alanine-glyoxylate transaminase (AGXT)

2.6.3: Oximinotransferases	Oximinotransferase

2.6.99: Other	Pyridoxine 5'-phosphate synthase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

AGXT

References

External links

Further reading