AGXT: Difference between revisions

From Wikipedia, the free encyclopedia
Browse history interactively
← Previous edit
Content deleted Content added
VisualWikitext
10.1007/978-1-4613-0381-7_73
Altered title. Add: isbn, date, chapter. Removed parameters. Put the {{Short description}} template first as prescribed by MOS:ORDER. Used lowercase "cite" template everywhere for consistency.
 
(20 intermediate revisions by 12 users not shown)
Line 1: Line 1:
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{PBB|geneid=189}}
{{cs1 config|name-list-style=vanc}}
⚫
'''Serine—pyruvate aminotransferase''' is an [[enzyme]] that in humans is encoded by the ''AGXT'' [[gene]].<ref name="pmid2039493">{{cite journal | author = 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 | author = 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 = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189| accessdate = }}</ref>
{{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 | 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 | 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}}</ref>


⚫
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"/>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->

{{PBB_Summary
==See also==
| section_title =
*[[Peroxisomal disorder]]
⚫
| 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 targeting, have been associated with type I primary [[hyperoxaluria]].<ref name="entrez"/>
}}


==References==
==References==
{{Reflist}}
{{Reflist}}

==External links==
==External links==
* [http://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=ph1 GeneReviews/NIH/NCBI/UW entry on Primary Hyperoxaluria Type 1]
* [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==
==Further reading==
{{Refbegin | 2}}
{{Refbegin | 2}}
⚫
*{{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 }}
{{PBB_Further_reading
*{{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 |doi-access= free }}
| 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 | 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 | 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=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 | author=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, 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 | author=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, 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|doi-access=free }}
*{{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=10.1083/jcb.111.6.2341 | pmc=2116406 }}
*{{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 |hdl=10271/960 |s2cid=953132 |hdl-access=free }}
*{{Cite journal | author=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=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= 10.1042/bj2680517| pmc=1131464 |display-authors=etal}}
*{{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=10.1111/j.1432-1033.1990.tb19420.x }}
*{{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 |s2cid=32933133 |doi-access= }}
*{{Cite journal | author=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, 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 |display-authors=etal}}
*{{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=10.1016/0014-5793(86)80563-4 }}
*{{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 | pmc=1682352 |display-authors=etal}}
*{{cite book | vauthors=Minatogawa Y, Kawai C, Hatada S, Sato M |chapter=Liver Specific Kynurenine (Alanine) |title=Recent Advances in Tryptophan Research |series=Adv. Exp. Med. Biol. |date=1996 |volume=398 |pages= 471–6 |pmid= 8906307 |doi= 10.1007/978-1-4613-0381-7_73 |isbn=978-1-4613-8026-9 }}
*{{Cite journal | author=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 | author=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=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 | 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= 10.1007/978-1-4613-0381-7_73 }}
*{{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 |s2cid=34307977 |display-authors=etal}}
*{{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=10.1136/jmg.34.6.489 | pmc=1050973 }}
*{{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 |s2cid=28076033 |display-authors=etal}}
*{{Cite journal | author=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=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-# |s2cid=196606396 }}
*{{Cite journal | author=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=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 |doi-access= free }}
*{{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}}
{{Refend}}
{{PDB Gallery|geneid=189}}
{{PDB Gallery|geneid=189}}



<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
⚫
{{Nitrogenous transferases}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}




{{gene-2-stub}}
{{gene-2-stub}}
⚫
{{Nitrogenous transferases}}

Latest revision as of 12:48, 24 January 2024

AGXT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAGXT, AGT, AGT1, AGXT1, PH1, SPAT, SPT, TLH6, alanine-glyoxylate aminotransferase, alanine--glyoxylate and serine--pyruvate aminotransferase, Ser-PyrAT
External IDsOMIM: 604285 MGI: 1329033 HomoloGene: 37251 GeneCards: AGXT
EC number2.6.1.44
Orthologs
SpeciesHumanMouse
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 MbChr 1: 93.06 – 93.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine—pyruvate aminotransferase is an enzyme that in humans is encoded by the AGXT gene.[5][6][7]

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.[7]

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172482 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026272 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b "Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)".

External links[edit]

Further reading[edit]



Stub icon

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

Retrieved from "https://en.wikipedia.org/w/index.php?title=AGXT&oldid=1198566314"