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{{Infobox_gene}}
'''Serine—pyruvate aminotransferase''' is an [[enzyme]] that in humans is encoded by the ''AGXT'' [[gene]].<ref name="pmid2039493">{{cite journal | vauthors = Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A | title = Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene | journal = Biochem Biophys Res Commun | volume = 176 | issue = 3 | pages = 1093–9 |date=Jul 1991 | pmid = 2039493 | pmc =  | doi =10.1016/0006-291X(91)90396-O  }}</ref><ref name="pmid2045108">{{cite journal | vauthors = Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ | title = Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase | journal = Genomics | volume = 10 | issue = 1 | pages = 34–42 |date=Jul 1991 | pmid = 2045108 | pmc =  | doi =10.1016/0888-7543(91)90481-S  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is expressed only in the liver and the encoded protein is localized mostly in the [[peroxisome]]s, where it is involved in [[glyoxylate]] detoxification. Mutations in this gene, some of which alter subcellular targeting, have been associated with [[Primary hyperoxaluria|type I primary]] [[hyperoxaluria]].<ref name="entrez"/>
}}
==See also==
*[[Peroxisomal disorder]]
==References==
{{Reflist}}
==External links==
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=ph1  GeneReviews/NIH/NCBI/UW entry on Primary Hyperoxaluria Type 1]
* {{UCSC gene info|AGT}}
* {{UCSC gene info|AGXT}}
==Further reading==
{{Refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{Cite journal  | author=Danpure CJ |title=Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. |journal=Biochimie |volume=75 |issue= 3–4 |pages= 309–15 |year= 1993 |pmid= 8507692 |doi=10.1016/0300-9084(93)90091-6  }}
*{{Cite journal  | author=Danpure CJ |title=Molecular etiology of primary hyperoxaluria type 1: new directions for treatment |journal=Am. J. Nephrol. |volume=25 |issue= 3 |pages= 303–10 |year= 2005 |pmid= 15961951 |doi= 10.1159/000086362 }}
*{{Cite journal  | vauthors=Minatogawa Y, Tone S, Allsop J |title=A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1 |journal=Hum. Mol. Genet. |volume=1 |issue= 8 |pages= 643–4 |year= 1993 |pmid= 1301173 |doi=10.1093/hmg/1.8.643  |display-authors=etal}}
*{{Cite journal  | vauthors=Purdue PE, Lumb MJ, Allsop J |title=A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1 |journal=Genomics |volume=13 |issue= 1 |pages= 215–8 |year= 1992 |pmid= 1349575 |doi=10.1016/0888-7543(92)90225-H  |display-authors=etal}}
*{{Cite journal  | vauthors=Purdue PE, Takada Y, Danpure CJ |title=Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1 |journal=J. Cell Biol. |volume=111 |issue= 6 Pt 1 |pages= 2341–51 |year= 1991 |pmid= 1703535 |doi=10.1083/jcb.111.6.2341  | pmc=2116406  }}
*{{Cite journal  | vauthors=Purdue PE, Allsop J, Isaya G |title=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 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10900–4 |year= 1992 |pmid= 1961759 |doi=10.1073/pnas.88.23.10900  | pmc=53039  |display-authors=etal}}
*{{Cite journal  | vauthors=Nishiyama K, Berstein G, Oda T, Ichiyama A |title=Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase |journal=Eur. J. Biochem. |volume=194 |issue= 1 |pages= 9–18 |year= 1991 |pmid= 2253628 |doi=10.1111/j.1432-1033.1990.tb19420.x  }}
*{{Cite journal  | vauthors=Takada Y, Kaneko N, Esumi H |title=Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon |journal=Biochem. J. |volume=268 |issue= 2 |pages= 517–20 |year= 1990 |pmid= 2363689 |doi=  | pmc=1131464  |display-authors=etal}}
*{{Cite journal  | vauthors=Danpure CJ, Jennings PR |title=Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I |journal=FEBS Lett. |volume=201 |issue= 1 |pages= 20–4 |year= 1986 |pmid= 3709805 |doi=10.1016/0014-5793(86)80563-4  }}
*{{Cite journal  | vauthors=Danpure CJ, Fryer P, Jennings PR |title=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 |journal=Eur. J. Cell Biol. |volume=64 |issue= 2 |pages= 295–313 |year= 1995 |pmid= 7813517 |doi=  |display-authors=etal}}
*{{Cite journal  | vauthors=Danpure CJ, Purdue PE, Fryer P |title=Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation |journal=Am. J. Hum. Genet. |volume=53 |issue= 2 |pages= 417–32 |year= 1993 |pmid= 8101040 |doi=  | pmc=1682352  |display-authors=etal}}
*{{Cite journal  | vauthors=Minatogawa Y, Kawai C, Hatada S, Sato M |title=Liver specific kynurenine(alanine):glyoxylate aminotransferase was expressed in kidney cell line |journal=Adv. Exp. Med. Biol. |volume=398 |issue=  |pages= 471–6 |year= 1997 |pmid= 8906307 |doi= 10.1007/978-1-4613-0381-7_73 }}
*{{Cite journal  | vauthors=von Schnakenburg C, Rumsby G |title=Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene |journal=J. Med. Genet. |volume=34 |issue= 6 |pages= 489–92 |year= 1997 |pmid= 9192270 |doi=10.1136/jmg.34.6.489  | pmc=1050973  }}
*{{Cite journal  | vauthors=Amoroso A, Pirulli D, Puzzer D |title=Gene symbol: AGXT. Disease: primary hyperoxaluria type I |journal=Hum. Genet. |volume=104 |issue= 5 |pages= 441 |year= 1999 |pmid= 10394939 |doi=10.1007/s004390050984  |display-authors=etal}}
*{{Cite journal  | vauthors=Pirulli D, Puzzer D, Ferri L |title=Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene |journal=Hum. Genet. |volume=104 |issue= 6 |pages= 523–5 |year= 1999 |pmid= 10453743 |doi=10.1007/s004390050998  |display-authors=etal}}
*{{Cite journal  | vauthors=Basmaison O, Rolland MO, Cochat P, Bozon D |title=Identification of 5 novel mutations in the AGXT gene |journal=Hum. Mutat. |volume=15 |issue= 6 |pages= 577 |year= 2000 |pmid= 10862087 |doi= 10.1002/1098-1004(200006)15:6<577::AID-HUMU9>3.0.CO;2-# }}
*{{Cite journal  | vauthors=Lumb MJ, Danpure CJ |title=Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36415–22 |year= 2000 |pmid= 10960483 |doi= 10.1074/jbc.M006693200 }}
}}
{{Refend}}
{{PDB Gallery|geneid=189}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Nitrogenous transferases}}
{{GNF_Protein_box
| image = PBB_Protein_AGXT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h0c.
| PDB = {{PDB2|1h0c}}, {{PDB2|1j04}}
| Name = Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)
| HGNCid = 341
| Symbol = AGXT
| AltSymbols =; AGT; AGT1; AGXT1; PH1; SPAT; SPT; TLH6
| OMIM = 604285
| ECnumber = 
| Homologene = 37251
| MGIid = 1329033
| GeneAtlas_image1 = PBB_GE_AGXT_206957_at_tn.png
| GeneAtlas_image2 = PBB_GE_AGXT_210327_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_AGXT_210326_at_tn.png
| Function = {{GNF_GO|id=GO:0004760 |text = serine-pyruvate transaminase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008453 |text = alanine-glyoxylate transaminase activity}} {{GNF_GO|id=GO:0008483 |text = transaminase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030170 |text = pyridoxal phosphate binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}}
| Process = {{GNF_GO|id=GO:0006625 |text = protein targeting to peroxisome}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0046487 |text = glyoxylate metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 189
    | Hs_Ensembl = ENSG00000172482
    | Hs_RefseqProtein = NP_000021
    | Hs_RefseqmRNA = NM_000030
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 241456835
    | Hs_GenLoc_end = 241467210
    | Hs_Uniprot = P21549
    | Mm_EntrezGene = 11611
    | Mm_Ensembl = ENSMUSG00000026272
    | Mm_RefseqmRNA = XM_981336
    | Mm_RefseqProtein = XP_986430
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 94965651
    | Mm_GenLoc_end = 94975813
    | Mm_Uniprot = Q3UEN9
  }}
}}
'''Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)''', also known as '''AGXT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189| accessdate = }}</ref>
 
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189| accessdate = }}</ref>
}}


==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Danpure CJ |title=Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. |journal=Biochimie |volume=75 |issue= 3-4 |pages= 309-15 |year= 1993 |pmid= 8507692 |doi=  }}
*{{cite journal  | author=Danpure CJ |title=Molecular etiology of primary hyperoxaluria type 1: new directions for treatment. |journal=Am. J. Nephrol. |volume=25 |issue= 3 |pages= 303-10 |year= 2005 |pmid= 15961951 |doi= 10.1159/000086362 }}
*{{cite journal  | author=Minatogawa Y, Tone S, Allsop J, ''et al.'' |title=A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. |journal=Hum. Mol. Genet. |volume=1 |issue= 8 |pages= 643-4 |year= 1993 |pmid= 1301173 |doi=  }}
*{{cite journal  | author=Purdue PE, Lumb MJ, Allsop J, ''et al.'' |title=A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. |journal=Genomics |volume=13 |issue= 1 |pages= 215-8 |year= 1992 |pmid= 1349575 |doi=  }}
*{{cite journal  | author=Purdue PE, Takada Y, Danpure CJ |title=Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. |journal=J. Cell Biol. |volume=111 |issue= 6 Pt 1 |pages= 2341-51 |year= 1991 |pmid= 1703535 |doi=  }}
*{{cite journal  | author=Purdue PE, Allsop J, Isaya G, ''et al.'' |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10900-4 |year= 1992 |pmid= 1961759 |doi=  }}
*{{cite journal  | author=Nishiyama K, Funai T, Katafuchi R, ''et al.'' |title=Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1093-9 |year= 1991 |pmid= 2039493 |doi=  }}
*{{cite journal  | author=Purdue PE, Lumb MJ, Fox M, ''et al.'' |title=Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. |journal=Genomics |volume=10 |issue= 1 |pages= 34-42 |year= 1991 |pmid= 2045108 |doi=  }}
*{{cite journal  | author=Nishiyama K, Berstein G, Oda T, Ichiyama A |title=Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. |journal=Eur. J. Biochem. |volume=194 |issue= 1 |pages= 9-18 |year= 1991 |pmid= 2253628 |doi=  }}
*{{cite journal  | author=Takada Y, Kaneko N, Esumi H, ''et al.'' |title=Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. |journal=Biochem. J. |volume=268 |issue= 2 |pages= 517-20 |year= 1990 |pmid= 2363689 |doi=  }}
*{{cite journal  | author=Danpure CJ, Jennings PR |title=Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I. |journal=FEBS Lett. |volume=201 |issue= 1 |pages= 20-4 |year= 1986 |pmid= 3709805 |doi=  }}
*{{cite journal  | author=Danpure CJ, Fryer P, Jennings PR, ''et al.'' |title=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. |journal=Eur. J. Cell Biol. |volume=64 |issue= 2 |pages= 295-313 |year= 1995 |pmid= 7813517 |doi=  }}
*{{cite journal  | author=Danpure CJ, Purdue PE, Fryer P, ''et al.'' |title=Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. |journal=Am. J. Hum. Genet. |volume=53 |issue= 2 |pages= 417-32 |year= 1993 |pmid= 8101040 |doi=  }}
*{{cite journal  | author=Minatogawa Y, Kawai C, Hatada S, Sato M |title=Liver specific kynurenine(alanine):glyoxylate aminotransferase was expressed in kidney cell line. |journal=Adv. Exp. Med. Biol. |volume=398 |issue=  |pages= 471-6 |year= 1997 |pmid= 8906307 |doi=  }}
*{{cite journal  | author=von Schnakenburg C, Rumsby G |title=Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. |journal=J. Med. Genet. |volume=34 |issue= 6 |pages= 489-92 |year= 1997 |pmid= 9192270 |doi=  }}
*{{cite journal  | author=Amoroso A, Pirulli D, Puzzer D, ''et al.'' |title=Gene symbol: AGXT. Disease: primary hyperoxaluria type I. |journal=Hum. Genet. |volume=104 |issue= 5 |pages= 441 |year= 1999 |pmid= 10394939 |doi=  }}
*{{cite journal  | author=Pirulli D, Puzzer D, Ferri L, ''et al.'' |title=Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene. |journal=Hum. Genet. |volume=104 |issue= 6 |pages= 523-5 |year= 1999 |pmid= 10453743 |doi=  }}
*{{cite journal  | author=Basmaison O, Rolland MO, Cochat P, Bozon D |title=Identification of 5 novel mutations in the AGXT gene. |journal=Hum. Mutat. |volume=15 |issue= 6 |pages= 577 |year= 2000 |pmid= 10862087 |doi= 10.1002/1098-1004(200006)15:6<577::AID-HUMU9>3.0.CO;2-# }}
*{{cite journal  | author=Lumb MJ, Danpure CJ |title=Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36415-22 |year= 2000 |pmid= 10960483 |doi= 10.1074/jbc.M006693200 }}
}}
{{refend}}


{{protein-stub}}
{{gene-2-stub}}
{{WikiDoc Sources}}

Latest revision as of 14:51, 25 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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]

See also

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)".

External links

Further reading



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