AGXT2

AGXT2
Identifiers
Aliases	AGXT2, AGT2, DAIBAT, alanine--glyoxylate aminotransferase 2, BAIBA
External IDs	OMIM: 612471; MGI: 2146052; HomoloGene: 12887; GeneCards: AGXT2; OMA:AGXT2 - orthologs
EC number	2.6.1.40
Gene location (Human)
Chr.	Chromosome 5 (human)
End	35,048,135 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	10,410,239 bp
RNA expression pattern
	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
	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
	64902
	268782
	ENSG00000113492
	ENSMUSG00000089678
	Q9BYV1
	Q3UEG6
	NM_001306173; NM_031900
	NM_001031851; NM_001310735; NM_001310736
	NP_001293102; NP_114106
	NP_001027021; NP_001297664; NP_001297665
	Wikidata
View/Edit Human	View/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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000113492 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000089678 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: Alanine--glyoxylate aminotransferase 2". Retrieved 2014-01-12.
^ [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##

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000113492 – Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[entrez-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##

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Function

References

Further reading