Skip to content

DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

Data

Loading the map…

Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

Select a territory to bring it forward.

Reading the map

Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

AKR1B1 reduces Glc to D-sorbitol

Glc + NADPH + H+ → D-sorbitol + NADP+

Reactome: R-HSA-5652172
Compartment: cytosol
Rhea: RHEA:59926

Inputs

GlcCHEBI:4167, C6H12O6, cytosol
NADPHCHEBI:57783, C21H26N7O17P3, cytosol
H+CHEBI:15378, H, cytosol

Outputs

D-sorbitolCHEBI:17924, C6H14O6, cytosol
NADP+CHEBI:58349, C21H25N7O17P3, cytosol

Catalysed by

aldose reductase (NADPH) activity of AKR1B1 [cytosol]EC 1.1.1.21; UniProt P15121

Literature

Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts Biochemistry, 1992
[Aldose reductase] Biochim. Biophys. Acta, 1960
Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes Eur. J. Biochem., 1993
Cloning and expression of human aldose reductase J. Biol. Chem., 1990
Aldose reductase, still a compelling target for diabetic neuropathy Curr Drug Targets, 2008
The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48 Acta Crystallogr. D Biol. Crystallogr., 2004