AGXT

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1H0C, 1J04, 2YOB, 3R9A, 4CBR, 4CBS, 4I8A, 4KXK, 4KYO

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

EC number

2.6.1.44

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2q37.3	Start	240,868,824 bp^[1]
Band	2q37.3	End	240,880,502 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1 D\|1 47.0 cM	Start	93,062,962 bp^[2]
Band	1 D\|1 47.0 cM	End	93,073,143 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right lobe of liver

kidney

kidney tubule

cerebellar vermis

renal medulla

renal cortex

spleen

glomerulus

metanephric glomerulus

jejunal mucosa

Top expressed in

left lobe of liver

gallbladder

sexually immature organism

duodenum

jejunum

submandibular gland

thoracic diaphragm

muscle tissue

pancreas

colon

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

^[3]

^[4]

Wikidata

View/Edit Human

View/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]

References

External links

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.

v t e PDB gallery
1h0c: THE CRYSTAL STRUCTURE OF HUMAN ALANINE:GLYOXYLATE AMINOTRANSFERASE 1j04: Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro

v t e Transferase: nitrogenous groups (EC 2.6)
2.6.1: Transaminases	Aspartate transaminase GOT1 GOT2 Alanine transaminase GABA transaminase Tyrosine aminotransferase Kynurenine—oxoglutarate transaminase Ornithine aminotransferase Branched-chain amino acid aminotransferase Alanine—glyoxylate transaminase AGXT
2.6.3: Oximinotransferases	Oximinotransferase
2.6.99: Other	Pyridoxine 5'-phosphate synthase

See also

References

External links

Further reading