AKR7A2

AKR7A2
Identifiers
Aliases	AKR7A2, AFAR, AFAR1, AFB1-AR1, AKR7, aldo-keto reductase family 7, member A2, aldo-keto reductase family 7 member A2
External IDs	OMIM: 603418; MGI: 107796; GeneCards: AKR7A2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2BP1
Gene location (Human)
Chr.	Chromosome 1 (human)
End	19,312,144 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	139,045,737 bp
RNA expression pattern
	Top expressed in
	mucosa of transverse colon; ; duodenum; ; right adrenal gland; ; right adrenal cortex; ; right uterine tube; ; left adrenal gland; ; jejunal mucosa; ; left adrenal cortex; ; human kidney; ; canal of the cervix;
	Top expressed in
	right kidney; ; proximal tubule; ; left lobe of liver; ; Paneth cell; ; human kidney; ; internal carotid artery; ; crypt of lieberkuhn of small intestine; ; external carotid artery; ; right ventricle; ; motor neuron;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	alditol:NADP+ 1-oxidoreductase activity; electron transfer activity; oxidoreductase activity; phenanthrene-9,10-epoxide hydrolase activity; aldo-keto reductase (NADP) activity; protein binding;
Cellular component	cytoplasm; Golgi apparatus; extracellular exosome; cytosol;
Biological process	xenobiotic metabolic process; cellular aldehyde metabolic process; daunorubicin metabolic process; doxorubicin metabolic process; carbohydrate metabolic process; electron transport chain;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	8574
	110198
	ENSG00000053371
	ENSMUSG00000028743
	O43488
	Q8CG76
	NM_003689; NM_001320979
	NM_025337
	NP_001307908; NP_003680
	NP_079613
	Wikidata
View/Edit Human	View/Edit Mouse

Aflatoxin B1 aldehyde reductase member 2 is an enzyme that in humans is encoded by the AKR7A2 gene.

Function

Aldo-keto reductases, such as AKR7A2, are involved in the detoxification of aldehydes and ketones.[supplied by OMIM]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000053371 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028743 – 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.
↑ Ireland LS, Harrison DJ, Neal GE, Hayes JD (Aug 1998). "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". Biochem J. 332 (1): 21–34. doi:10.1042/bj3320021. PMC 1219447. PMID 9576847.
1 2 "Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)".

External links

Human AKR7A2 genome location and AKR7A2 gene details page in the UCSC Genome Browser.
Overview of all the structural information available in the PDB for UniProt: O43488 (Human Aflatoxin B1 aldehyde reductase member 2 (AKR7A2)) at the PDBe-KB.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000053371 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028743 – 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.

[pmid9576847-5] Ireland LS, Harrison DJ, Neal GE, Hayes JD (Aug 1998). "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". Biochem J. 332 (1): 21–34. doi:10.1042/bj3320021. PMC 1219447. PMID 9576847.

[entrez-6] 1 2 "Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)".

v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase 6-Phosphogluconate dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Alcohol oxidase Glucose oxidase L-gulonolactone oxidase L-lactate oxidase Xanthine oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

AKR7A2

Function

See also

References

Further reading

External links