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AGXT2

Introduction

The human AGXT2 gene encodes the protein Alanine—glyoxylate aminotransferase 2. [1]

Function

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.[2]

References

References

  1. ↑ “Entrez Gene: Alanine–glyoxylate aminotransferase 2”. Retrieved 2014-01-12.
  2. ↑ [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

Further reading

  • Lee, I. S.; Muragaki, Y.; Ideguchi, T.; Hase, T.; Tsuji, M.; Ooshima, A.; Okuno, E.; Kido, R. (1995). “Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney”. Journal of Biochemistry. 117 (4): 856–862. PMID 7592550.
  • Nicholson, G.; Rantalainen, M.; Li, J. V.; Maher, A. D.; Malmodin, D.; Ahmadi, K. R.; Faber, J. H.; Barrett, A.; Min, J. L.; Rayner, N. W.; Toft, H.; Krestyaninova, M.; Viksna, J.; Neogi, S. G.; Dumas, M. E.; Sarkans, U.; Molpage, P.; Donnelly, T.; Illig, J.; Adamski, K.; Suhre, M.; Allen, K. T.; Zondervan, T. D.; Spector, J. K.; Nicholson, J. C.; Lindon, D.; Baunsgaard, E.; Holmes, M. I.; McCarthy, C. C.; Holmes, C. C. (2011). Barsh, Gregory S, 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.; Wasner, C.; Krebs, A.; Kronenberg, F.; Chang, D.; Meisinger, C.; Wichmann, H. E.; Hoffmann, W.; Völzke, H.; Völker, U.; Teumer, A.; Biffar, R.; Kocher, T.; Felix, S. B.; Illig, T.; Kroemer, H. K.; Gieger, C.; Römisch-Margl, W.; Nauck, M. (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.
  • Rodionov, R. N.; Murry, D. J.; Vaulman, S. F.; Stevens, J. W.; Lentz, S. R. (2009). “Human Alanine-Glyoxylate Aminotransferase 2 Lowers Asymmetric Dimethylarginine and Protects from Inhibition of Nitric Oxide Production”. Journal of Biological Chemistry. 285 (8): 5385–5391. doi:10.1074/jbc.M109.091280. PMC 2820767. PMID 20018850.
  • Baker, P. R. S.; Cramer, S. D.; Kennedy, M.; Assimos, D. G.; Holmes, R. P. (2004). “Glycolate and glyoxylate metabolism in HepG2 cells”. AJP: Cell Physiology. 287 (5): C1359–C1365. doi:10.1152/ajpcell.00238.2004. PMID 15240345.
  • Danpure, C. J. (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.; Salama, A.; Wheeler, D. C.; Leiper, J.; Leiper, J. (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.