page_title: Aldose reductase
section_title: Enzyme structure
hierarchical_section_title: Aldose reductase / Enzyme structure
context_page_description: In enzymology, aldose reductase is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. It is primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism.
context_section_description: Aldose reductase may be considered a prototypical enzyme of the aldo-keto reductase enzyme superfamily. The enzyme comprises 315 amino acid residues and folds into a β/α-barrel structural motif composed of eight parallel β strands. Adjacent strands are connected by eight peripheral α-helical segments running anti-parallel to the β sheet. The catalytic active site situated in the barrel core. The NADPH cofactor is situated at the top of the β/α barrel, with the nicotinamide ring projects down in the center of the barrel and pyrophosphate straddling the barrel lip.
caption: Role of aldehyde reductase (shown in yellow box) in norepinephrine degradation, contributing in the creation of MHPG, a minor catecholamine metabolite.[7]