AKR1B10

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1ZUA, 4GA8, 4GAB, 4GQ0, 4GQG, 4I5X, 4ICC, 4JIH, 4JII, 4WEV, 4XZL, 4XZN, 4XZM

Identifiers

Aliases

AKR1B10, AKR1B11, AKR1B12, ALDRLn, ARL-1, ARL1, HIS, HSI, aldo-keto reductase family 1, member B10 (aldose reductase), aldo-keto reductase family 1 member B10

External IDs

MGI: 107673 HomoloGene: 116462 GeneCards: AKR1B10

Gene ontology
Molecular function	• retinal dehydrogenase activity • geranylgeranyl reductase activity • indanol dehydrogenase activity • aldo-keto reductase (NADP) activity • protein binding • oxidoreductase activity
Cellular component	• cytosol • extracellular region • lysosome • extracellular exosome
Biological process	• steroid metabolic process • daunorubicin metabolic process • doxorubicin metabolic process • digestion • retinoid metabolic process • farnesol catabolic process • cellular aldehyde metabolic process • oxidation-reduction process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


57016


14187

Ensembl


ENSG00000198074


ENSMUSG00000029762

UniProt


O60218


P45377

RefSeq (mRNA)


NM_020299


NM_008012

RefSeq (protein)


NP_064695.3


NP_032038.1

Location (UCSC)

Chr 7: 134.53 – 134.54 Mb

Chr 6: 34.35 – 34.37 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Aldo-keto reductase family 1 member B10 is an enzyme that in humans is encoded by the AKR1B10 gene.^[3]^[4]^[5]

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member can efficiently reduce aliphatic and aromatic aldehydes, and it is less active on hexoses. It is highly expressed in adrenal gland, small intestine, and colon, and may play an important role in liver carcinogenesis.^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Hyndman DJ, Flynn TG (Oct 1998). "Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family". Biochim Biophys Acta. 1399 (2–3): 198–202. doi:10.1016/s0167-4781(98)00109-2. PMID 9765596.
↑ Cao D, Fan ST, Chung SS (Jun 1998). "Identification and characterization of a novel human aldose reductase-like gene". J Biol Chem. 273 (19): 11429–35. doi:10.1074/jbc.273.19.11429. PMID 9565553.
1 2 "Entrez Gene: AKR1B10 aldo-keto reductase family 1, member B10 (aldose reductase)".

External links

Human AKR1B10 genome location and AKR1B10 gene details page in the UCSC Genome Browser.
Human ARL1 genome location and ARL1 gene details page in the UCSC Genome Browser.

Scuric Z, Stain SC, Anderson WF, Hwang JJ (1998). "New member of aldose reductase family proteins overexpressed in human hepatocellular carcinoma". Hepatology. 27 (4): 943–50. doi:10.1002/hep.510270408. PMID 9537432.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Crosas B, Hyndman DJ, Gallego O, et al. (2003). "Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism". Biochem. J. 373 (Pt 3): 973–9. doi:10.1042/BJ20021818. PMC 1223539. PMID 12732097.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Petrovic MG, Peterlin B, Hawlina M, Petrovic D (2005). "Aldose reductase (AC)n gene polymorphism and susceptibility to diabetic retinopathy in Type 2 diabetes in Caucasians". J. Diabetes Complicat. 19 (2): 70–3. doi:10.1016/j.jdiacomp.2004.08.004. PMID 15745835.
Kang ES, Kim HJ, Paek KS, et al. (2005). "Phorbol ester up-regulates aldose reductase expression in A549 cells: a potential role for aldose reductase in cell cycle modulation". Cell. Mol. Life Sci. 62 (10): 1146–55. doi:10.1007/s00018-005-5024-4. PMID 15928807.
Lee YS, Paek KS, Kang ES, et al. (2005). "Involvement of nuclear factor kappaB in up-regulation of aldose reductase gene expression by 12-O-tetradecanoylphorbol-13-acetate in HeLa cells". Int. J. Biochem. Cell Biol. 37 (11): 2297–309. doi:10.1016/j.biocel.2005.04.016. PMID 15936242.
Vikramadithyan RK, Hu Y, Noh HL, et al. (2005). "Human aldose reductase expression accelerates diabetic atherosclerosis in transgenic mice". J. Clin. Invest. 115 (9): 2434–43. doi:10.1172/JCI24819. PMC 1190371. PMID 16127462.
Hazemann I, Dauvergne MT, Blakeley MP, et al. (2005). "High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase". Acta Crystallogr. D. 61 (Pt 10): 1413–7. doi:10.1107/S0907444905024285. PMID 16204895.
Mashkova TD, Oparina NIu, Zinov'eva OL, et al. (2007). "[Transcription TIMP3, DAPk1 and AKR1B10 genes in squamous cell lung cancer]". Mol. Biol. (Mosk.). 40 (6): 1047–54. doi:10.1134/s0026893306060148. PMID 17209433.
Tammali R, Ramana KV, Srivastava SK (2007). "Aldose reductase regulates TNF-alpha-induced PGE2 production in human colon cancer cells". Cancer Lett. 252 (2): 299–306. doi:10.1016/j.canlet.2007.01.001. PMC 1945127. PMID 17300864.
Yan R, Zu X, Ma J, et al. (2007). "Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: Implication for cancer intervention". Int. J. Cancer. 121 (10): 2301–6. doi:10.1002/ijc.22933. PMID 17597105.

PDB gallery

1zua: Crystal Structure Of AKR1B10 Complexed With NADP+ And Tolrestat

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA 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+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone 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

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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AKR1B10

References

External links

Further reading