| Name | aldo keto reductase (protein family or complex) |
|---|---|
| Synonyms | aldo keto reductase; aldo keto reductases |
| Name | acrolein |
|---|---|
| CAS | 2-propenal |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 14673659 | Iuchi Y, Kaneko T, Matsuki S, Ishii T, Ikeda Y, Uchida K, Fujii J: Carbonyl stress and detoxification ability in the male genital tract and testis of rats. Histochem Cell Biol. 2004 Feb;121(2):123-30. Epub 2003 Dec 13. The aldo-keto reductase (AKR) family of enzymes catalyze the reductive detoxification of various carbonyl compounds in an -dependent manner. Virtually the same cells were stained with a monoclonal antibody (mAb) 5F6, raised against an acrolein-modified protein. |
1(0,0,0,1) | Details |
| 8183257 | Kolb NS, Hunsaker LA, Vander Jagt DL: Aldose reductase-catalyzed reduction of acrolein: implications in cyclophosphamide toxicity. Mol Pharmacol. 1994 Apr;45(4):797-801. Aldose reductase (EC 1.1.1.21), a member of the aldo-keto reductase superfamily, catalyzes the -dependent reduction of acrolein to allyl (Km = 80 microM, kcat = 87 min-1). |
81(1,1,1,1) | Details |
| 15019089 | Gardner R, Kazi S, Ellis EM: Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase. Toxicol Lett. 2004 Mar 14;148(1-2):65-72. |
7(0,0,1,2) | Details |
| 17597105 | Yan R, Zu X, Ma J, Liu Z, Adeyanju M, Cao D: Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: Implication for cancer intervention. Int J Cancer. 2007 Nov 15;121(10):2301-6. Recombinant AKR1B10 protein showed strong enzymatic activity to acrolein and crotonaldehyde, with K (m) = 110.1 +/- 12.2 microM and V (max) = 3,122.0 +/- 64.7 nmol/mg protein/min for acrolein and K (m) = 86.7 +/- 14.3 microM and V (max) = 2,647.5 +/- 132.2 nmol/mg protein/min for crotonaldehyde. |
2(0,0,0,2) | Details |
| 18845131 | Endo S, Matsunaga T, Mamiya H, Hara A, Kitade Y, Tajima K, El-Kabbani O: Characterization of a rat -dependent aldo-keto reductase (AKR1B13) induced by oxidative stress. Chem Biol Interact. 2009 Mar 16;178(1-3):151-7. Epub 2008 Sep 19. Recombinant AKR1B13 exhibited -linked reductase activity towards various aldehydes and alpha-dicarbonyl compounds, which include reactive compounds such as glyoxal, acrolein, and 3-deoxyglucosone. |
2(0,0,0,2) | Details |
| 12604212 | Hinshelwood A, McGarvie G, Ellis EM: Substrate specificity of mouse aldo-keto reductase AKR7A5. Chem Biol Interact. 2003 Feb 1;143-144:263-9. It has low specific activity towards ketones, and alpha,beta-unsaturated carbonyls such as acrolein and 4-hydroxynonal. |
2(0,0,0,2) | Details |
| 19608619 | MacLeod AK, McMahon M, Plummer SM, Higgins LG, Penning TM, Igarashi K, Hayes JD: Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds. Carcinogenesis. 2009 Sep;30(9):1571-80. Epub 2009 Jul 16. Whole-genome microarray revealed that knockdown of KEAP1 resulted in 23 messenger RNAs (mRNAs) being up-regulated > or = 2.0-fold. mRNA for aldo-keto reductase (AKR) 1B10, AKR1C1, AKR1C2 and AKR1C3 were induced to the greatest extent, showing increases of between 12- and 16-fold, whereas mRNA for glutamate-cysteine ligase catalytic and modifier subunits, NAD (P) H:quinone oxidoreductase-1 and haem oxygenase-1 (HMOX1) were induced between 2.0- and 4.8-fold. Activation of NRF2, by KEAP1 knockdown, caused a 75% increase in the amount of in HaCaT cells and a 1.4- to 1.6-fold increase in their resistance to the electrophiles acrolein, chlorambucil and cumene hydroperoxide (CuOOH), as well as the redox-cycling agent |
1(0,0,0,1) | Details |
| 10764810 | Dixit BL, Balendiran GK, Watowich SJ, Srivastava S, Ramana KV, Petrash JM, Bhatnagar A, Srivastava SK: Kinetic and structural characterization of the -binding site of aldose reductase. J Biol Chem. 2000 Jul 14;275(28):21587-95. The catalytic efficiency of AR in the reduction of the conjugates of acrolein, trans-2-hexenal, trans-2-nonenal, and trans,trans-2,4-decadienal was 4-1000-fold higher than for the corresponding free alkanal. Aldose reductase (AR), a member of the aldo-keto reductase superfamily, has been implicated in the etiology of secondary diabetic complications. |
2(0,0,0,2) | Details |
| 9890881 | Srivastava S, Watowich SJ, Petrash JM, Srivastava SK, Bhatnagar A: Structural and kinetic determinants of reduction by aldose reductase. Biochemistry. 1999 Jan 5;38(1):42-54. Aldose reductase (AR) is a member of the aldo-keto reductase superfamily. Short-chain aldehydes such as and acrolein were reduced less efficiently. |
1(0,0,0,1) | Details |