View source for AKR7A2

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Aflatoxin B1 [[aldehyde reductase]] member 2''' is an [[enzyme]] that in [[human]]s is encoded by the ''AKR7A2'' [[gene]].<ref name="pmid9576847">{{cite journal | vauthors = Ireland LS, Harrison DJ, Neal GE, Hayes JD | title = Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase | journal = Biochem J | volume = 332 | issue =  1| pages = 21–34 |date=Aug 1998 | pmid = 9576847 | pmc = 1219447 | doi =  10.1042/bj3320021}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8574}}</ref>
== Function ==
[[Aldo-keto reductase]]s, such as AKR7A2, are involved in the [[detoxification]] of [[aldehyde]]s and [[ketone]]s.[supplied by OMIM]<ref name="entrez"/>
==References==
{{reflist}}
==External links==
* {{UCSC gene info|AKR7A2}}
* {{PDBe-KB2|O43488|Human Aflatoxin B1 aldehyde reductase member 2 (AKR7A2)}}
==Further reading==
{{refbegin | 2}}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | vauthors=Praml C, Savelyeva L, Perri P, Schwab M |title=Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1 in a region frequently altered in human tumor cells |journal=Cancer Res. |volume=58 |issue= 22 |pages= 5014–8 |year= 1998 |pmid= 9823300 }}
*{{cite journal  | vauthors=Kelly VP, Sherratt PJ, Crouch DH, Hayes JD |title=Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 847–61 |year= 2002 |pmid= 12071861 |doi= 10.1042/BJ20020342  | pmc=1222835 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
*{{cite journal  | vauthors=Praml C, Savelyeva L, Schwab M |title=Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells |journal=Oncogene |volume=22 |issue= 30 |pages= 4765–73 |year= 2003 |pmid= 12879023 |doi= 10.1038/sj.onc.1206684 |doi-access= free }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R |s2cid=4427026 |display-authors=etal}}
*{{cite journal  | vauthors=Jordanova A, Irobi J, Thomas FP |title=Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy |journal=Nat. Genet. |volume=38 |issue= 2 |pages= 197–202 |year= 2006 |pmid= 16429158 |doi= 10.1038/ng1727 |s2cid=16668375 |display-authors=etal|url=https://lirias.kuleuven.be/handle/123456789/8070 }}
*{{cite journal  | vauthors=Gregory SG, Barlow KF, McLay KE |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G |display-authors=etal|doi-access=free }}
*{{cite journal  | vauthors=Lyon RC, Johnston SM, Watson DG |title=Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2 |journal=J. Biol. Chem. |volume=282 |issue= 36 |pages= 25986–92 |year= 2007 |pmid= 17591773 |doi= 10.1074/jbc.M702465200 |display-authors=etal|doi-access=free }}
{{refend}}
{{PDB Gallery|geneid=8574}}
{{Alcohol oxidoreductases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
[[Category:EC 1.1.1]]
[[Category:Gamma-Hydroxybutyric acid]]
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