DCXR Human, Bioactive
Description
Introduction to DCXR Human, Bioactive
DCXR Human, Bioactive is a recombinant human enzyme produced in E. coli, representing the functional form of dicarbonyl/L-xylulose reductase (EC 1.1.1.10). It is a single non-glycosylated polypeptide chain (264 amino acids) fused to an N-terminal His-Tag for purification . This enzyme catalyzes the NADPH-dependent reduction of α-dicarbonyl compounds, pentoses, and L-xylulose, playing critical roles in carbohydrate metabolism and detoxification .
Enzymatic Function
DCXR participates in the uronate cycle, converting L-xylulose to xylitol, an osmolyte critical for renal tubule osmoregulation . It also detoxifies α-dicarbonyl compounds (e.g., methylglyoxal) via reduction, mitigating oxidative stress .
Role in Metabolism
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Glycolysis Regulation: DCXR promotes aerobic glycolysis in cancer cells by enhancing ATP and lactate production .
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Cell Cycle Control: Overexpression accelerates G1/S phase progression, while knockdown arrests cells in G0/G1 .
Disease Implications
Breast Cancer Studies
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Knockdown Experiments:
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Glycolysis Inhibition: 2-DG abrogates DCXR-induced proliferation in MDA-MB-231 cells .
Renal Cell Carcinoma
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Overexpression Effects:
Diagnostic/Prognostic Potential
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Breast Cancer: DCXR upregulation correlates with tumor size, stage, and metastasis, suggesting utility as a biomarker .
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Renal Cell Carcinoma: Low DCXR expression may predict aggressive disease; therapeutic overexpression warrants investigation .
Treatment Targets
Product Specs
Product Science Overview
Dicarbonyl/L-Xylulose Reductase (DCXR), also known as Carbonyl Reductase II, is an enzyme that plays a crucial role in the metabolism of various sugars and carbonyl compounds. This enzyme is particularly significant in the reduction of L-xylulose and other dicarbonyl compounds, which are intermediates in the uronate cycle of glucose metabolism .
The human recombinant form of DCXR is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain consisting of 264 amino acids. The recombinant enzyme includes a 20 amino acid His-Tag at the N-terminus, which facilitates its purification through chromatographic techniques . The molecular mass of the enzyme is approximately 28 kDa .
DCXR catalyzes the NADPH-dependent reduction of a variety of pentoses, tetroses, trioses, alpha-dicarbonyl molecules, and L-xylulose. This reduction process is essential for the conversion of these compounds into their respective alcohol forms, such as xylitol from L-xylulose . The enzyme’s activity is crucial for maintaining cellular osmoregulation and water absorption in the proximal renal tubules by producing xylitol, an osmolyte that prevents osmolytic stress .
The enzyme’s role in the uronate cycle of glucose metabolism highlights its importance in the broader context of carbohydrate metabolism. By converting L-xylulose to xylitol, DCXR helps regulate the levels of reactive carbonyl species, which can be harmful if accumulated in high concentrations . Additionally, the enzyme’s activity in the kidneys aids in the prevention of osmolytic stress, thereby contributing to overall renal health .
The recombinant DCXR enzyme is typically stored in a sterile, filtered, colorless solution containing Tris-HCl buffer, dithiothreitol (DTT), glycerol, and sodium chloride (NaCl). For short-term storage, the enzyme can be kept at 4°C, while long-term storage requires freezing at -20°C with the addition of a carrier protein to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity and stability .
DCXR has various applications in biochemical research and clinical studies. Its ability to reduce a wide range of carbonyl compounds makes it a valuable tool for studying metabolic pathways and the effects of reactive carbonyl species. Additionally, the enzyme’s role in osmoregulation and renal function can be explored in the context of kidney health and disease .
