AGXT2

Protein-coding gene in the species Homo sapiens
AGXT2
Identifiers
AliasesAGXT2, AGT2, DAIBAT, alanine--glyoxylate aminotransferase 2, BAIBA
External IDsOMIM: 612471; MGI: 2146052; HomoloGene: 12887; GeneCards: AGXT2; OMA:AGXT2 - orthologs
EC number2.6.1.40
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for AGXT2
Genomic location for AGXT2
Band5p13.2Start34,998,101 bp[1]
End35,048,135 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for AGXT2
Genomic location for AGXT2
Band15|15 A1Start10,358,618 bp[2]
End10,410,239 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • renal medulla

  • renal cortex

  • human kidney

  • buccal mucosa cell

  • jejunal mucosa

  • gallbladder

  • duodenum

  • caput epididymis

  • muscle tissue
Top expressed in
  • left lobe of liver

  • right kidney

  • human kidney

  • proximal tubule

  • embryo

  • yolk sac

  • islet of Langerhans

  • ureter

  • duodenum

  • primary visual cortex
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • transferase activity
  • (R)-3-amino-2-methylpropionate-pyruvate transaminase activity
  • pyridoxal phosphate binding
  • catalytic activity
  • alanine-glyoxylate transaminase activity
  • identical protein binding
  • transaminase activity
Cellular component
  • mitochondrial matrix
  • mitochondrion
Biological process
  • glycine biosynthetic process, by transamination of glyoxylate
  • positive regulation of nitric oxide biosynthetic process
  • glyoxylate catabolic process
  • L-alanine catabolic process, by transamination
  • glyoxylate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

64902

268782

Ensembl

ENSG00000113492

ENSMUSG00000089678

UniProt

Q9BYV1

Q3UEG6

RefSeq (mRNA)

NM_001306173
NM_031900

NM_001031851
NM_001310735
NM_001310736

RefSeq (protein)

NP_001293102
NP_114106

NP_001027021
NP_001297664
NP_001297665

Location (UCSC)Chr 5: 35 – 35.05 MbChr 15: 10.36 – 10.41 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The human AGXT2 gene encodes the protein Alanine—glyoxylate aminotransferase 2. [5]

Function

The protein encoded by this gene is a class III pyridoxal-phosphate-dependent mitochondrial aminotransferase. It catalyzes the conversion of glyoxylate to glycine using L-alanine as the amino donor.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000113492 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000089678 – 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. ^ "Entrez Gene: Alanine--glyoxylate aminotransferase 2". Retrieved 2014-01-12.
  6. ^ [provided by RefSeq, Dec 2008]. ##Evidence-Data-START## Transcript exon combination :: AJ292204.1, AB193309.1 [ECO:0000332] RNAseq introns  :: mixed/partial sample support ERS025084, ERS025088 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## gene product(s) localized to mito. :: reported by MitoCarta ##RefSeq-Attributes-END##

Further reading

  • Lee IS, Muragaki Y, Ideguchi T, Hase T, Tsuji M, Ooshima A, et al. (April 1995). "Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney". Journal of Biochemistry. 117 (4): 856–862. doi:10.1093/oxfordjournals.jbchem.a124787. PMID 7592550.
  • Nicholson G, Rantalainen M, Li JV, Maher AD, Malmodin D, Ahmadi KR, et al. (September 2011). Barsh GS (ed.). "A genome-wide metabolic QTL analysis in Europeans implicates two loci shaped by recent positive selection". PLOS Genetics. 7 (9): e1002270. doi:10.1371/journal.pgen.1002270. PMC 3169529. PMID 21931564.
  • Suhre K, Wallaschofski H, Raffler J, Friedrich N, Haring R, Michael K, et al. (June 2011). "A genome-wide association study of metabolic traits in human urine". Nature Genetics. 43 (6): 565–569. doi:10.1038/ng.837. PMID 21572414. S2CID 28694666.
  • Rodionov RN, Murry DJ, Vaulman SF, Stevens JW, Lentz SR (February 2010). "Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production". The Journal of Biological Chemistry. 285 (8): 5385–5391. doi:10.1074/jbc.M109.091280. PMC 2820767. PMID 20018850.
  • Baker PR, Cramer SD, Kennedy M, Assimos DG, Holmes RP (November 2004). "Glycolate and glyoxylate metabolism in HepG2 cells". American Journal of Physiology. Cell Physiology. 287 (5): C1359–C1365. doi:10.1152/ajpcell.00238.2004. PMID 15240345.
  • Danpure CJ (August 2005). "Primary hyperoxaluria: from gene defects to designer drugs?". Nephrology, Dialysis, Transplantation. 20 (8): 1525–1529. doi:10.1093/ndt/gfh923. PMID 15956068.
  • Caplin B, Wang Z, Slaviero A, Tomlinson J, Dowsett L, Delahaye M, et al. (December 2012). "Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure". Arteriosclerosis, Thrombosis, and Vascular Biology. 32 (12): 2892–2900. doi:10.1161/ATVBAHA.112.254078. PMID 23023372.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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