Search results for AKR1B1

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Reaction (3 results from a total of 3)

Identifier: R-HSA-5652172
Species: Homo sapiens
Compartment: cytosol
Cytosolic AKR1B1 (aldose reductase) catalyzes the reaction of glucose (Glc) and NADPH + H+ to form D-sorbitol and NADP+. This reaction was first described by Hers (1960) in sheep seminal vesicles; the human enzyme was identified by Nishimura et al. (1990) and is a potential target for treatment of diabetic neuropathy (Oates, 2008). The active enzyme is a monomer (Ruiz et al. 2004) whose amino-terminal methionine residue has been removed (Jacquinod et al. 1993). Under physiological conditions, formation of D-sorbitol is strongly favored (Grimshaw 1992).
Identifier: R-HSA-5696822
Species: Homo sapiens
Compartment: mitochondrial matrix
The aldo-keto reductases (AKRs) are multifunctional enzymes that catalyse the reduction of biogenic and xenobiotic aldehydes and ketones as well as the synthesis and metabolism of sex hormones. The newest identified member, Aldo-keto reductase family 1 member B15 (AKR1B15) is able to catalyse the reduction of 17beta-sex hormones such as 17beta-estradiol (EST17b) to estrone (E1). Two isoforms of AKR1B15 exist in different subcellular locations; isoform 2 is cytosolic (like most AKRs) whereas isoform 1 co-localises with the mitochondria (Weber et al. 2015).
Identifier: R-HSA-196060
Species: Homo sapiens
Compartment: cytosol
Isocaproaldehyde is reduced by NADPH + H+ to yield 4-methylpentan-1-ol and NADP+. This cytosolic reaction is catalyzed by AKR1B1 (aldose reductase). The purified human enzyme has been shown to catalyze this reaction efficiently in vitro; its abundance in adrenal tissue in humans and other mammals and its concordant expression with other enzymes of steroid hormone synthesis are consistent with it performing this role in vivo as well (Matsuura et al. 1996; Lefrancois-Martinez et al. 2004). The metabolic fate of 4-methylpentan-1-ol is unknown.
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