AGXT

From Wikipedia, the free encyclopedia

Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)

PDB rendering based on 1h0c.

Available structures: 1h0c, 1j04

Identifiers

Symbol(s)

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

External IDs

OMIM: 604285 MGI: 1329033 HomoloGene: 37251

Gene ontology
Molecular Function:	• serine-pyruvate transaminase activity • protein binding • alanine-glyoxylate transaminase activity • transaminase activity • transferase activity • pyridoxal phosphate binding • protein homodimerization activity
Cellular Component:	• mitochondrion • peroxisome
Biological Process:	• protein targeting to peroxisome • metabolic process • glyoxylate metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000030 (mRNA)
NP_000021 (protein)

XM_981336 (mRNA)
XP_986430 (protein)

Location

Chr 2: 241.46 - 241.47 Mb

Chr 1: 94.97 - 94.98 Mb

Pubmed search

[1]

[2]

Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase), also known as AGXT, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase).

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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. 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.
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.
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.