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Literature summary extracted from

  • Balestri, F.; Cappiello, M.; Moschini, R.; Rotondo, R.; Abate, M.; Del-Corso, A.; Mura, U.
    Modulation of aldose reductase activity by aldose hemiacetals (2015), Biochim. Biophys. Acta, 1850, 2329-2339.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.21 drug development development of reductase inhibitors as drugs counteracting the onset of diabetic complications Homo sapiens
1.1.1.21 drug development development of reductase inhibitors as drugs counteracting the onset of diabetic complications Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.21 additional information partial nonclassical competitive inhibition is exerted by the aldose hemiacetal on the reduction of the free aldehyde, aldose reductase modulation by hemiacetals, negative cooperative behavior of AR acting on L-idose, mechanism of inhibition, kinetic modelling, nonclassical competitive model, detailed overview Bos taurus
1.1.1.21 additional information partial nonclassical competitive inhibition is exerted by the aldose hemiacetal on the reduction of the free aldehyde, aldose reductase modulation by hemiacetals, negative cooperative behavior of AR acting on L-idose, mechanism of inhibition, kinetic modelling, nonclassical competitive model, detailed overview Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.21 additional information
-
additional information the enzyme generates non-hyperbolic kinetics, mimicking a negative cooperative behavior, due to the simultaneous action of two enzyme forms acting on the same substrate. The apparent cooperative behavior of AR acting on glucose and other hexoses and pentoses, but not on tethroses, glyceraldehyde, 4-hydroxynonenal and 4-nitrobenzaldehyde, is generated by a partial nonclassical competitive inhibition exerted by the aldose hemiacetal on the reduction of the free aldehyde, Michaelis-Menten kinetic modelling with substrate L-idose, nonclassical competitive model, detailed overview Homo sapiens
1.1.1.21 additional information
-
additional information the enzyme generates non-hyperbolic kinetics, mimicking a negative cooperative behavior, due to the simultaneous action of two enzyme forms acting on the same substrate. The apparent cooperative behavior of AR acting on glucose and other hexoses and pentoses, but not on tethroses, glyceraldehyde, 4-hydroxynonenal and 4-nitrobenzaldehyde, is generated by a partial nonclassical competitive inhibition exerted by the aldose hemiacetal on the reduction of the free aldehyde, Michaelis-Menten kinetic modelling with substrate L-idose, nonclassical competitive model, detailed overview Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.21 34000
-
x * 34000, about, SDS-PAGE Homo sapiens
1.1.1.21 34000
-
x * 34000, about, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.21 D-glucose + NADPH + H+ Homo sapiens
-
D-sorbitol + NADP+
-
?
1.1.1.21 D-glucose + NADPH + H+ Bos taurus
-
D-sorbitol + NADP+
-
?
1.1.1.21 additional information Homo sapiens due to the unavoidable presence of the hemiacetal, glucose reduction by aldose reductase occurs under different conditions with respect to other relevant enzyme substrates, such as alkanals and alkenals, coming from membrane lipid peroxidation ?
-
?
1.1.1.21 additional information Bos taurus due to the unavoidable presence of the hemiacetal, glucose reduction by aldose reductase occurs under different conditions with respect to other relevant enzyme substrates, such as alkanals and alkenals, coming from membrane lipid peroxidation ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.21 Bos taurus P16116
-
-
1.1.1.21 Homo sapiens P15121
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.21 lens
-
Bos taurus
-
1.1.1.21 additional information purified recombinant enzyme Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.21 4-nitrobenzaldehyde + NADPH + H+
-
Homo sapiens 4-nitrobenzyl alcohol + NADP+
-
?
1.1.1.21 4-nitrobenzaldehyde + NADPH + H+
-
Bos taurus ?
-
?
1.1.1.21 D-erythrose + NADPH + H+
-
Homo sapiens ?
-
?
1.1.1.21 D-erythrose + NADPH + H+
-
Bos taurus ?
-
?
1.1.1.21 D-galactose + NADPH + H+
-
Homo sapiens ?
-
?
1.1.1.21 D-galactose + NADPH + H+
-
Bos taurus ?
-
?
1.1.1.21 D-glucose + NADPH + H+
-
Homo sapiens D-sorbitol + NADP+
-
?
1.1.1.21 D-glucose + NADPH + H+
-
Bos taurus D-sorbitol + NADP+
-
?
1.1.1.21 D-ribose + NADPH + H+
-
Homo sapiens ?
-
?
1.1.1.21 D-ribose + NADPH + H+
-
Bos taurus ?
-
?
1.1.1.21 D-xylose + NADPH + H+
-
Homo sapiens ?
-
?
1.1.1.21 D-xylose + NADPH + H+
-
Bos taurus ?
-
?
1.1.1.21 DL-glyceraldehyde + NADPH + H+
-
Homo sapiens glycerol + NADP+
-
?
1.1.1.21 DL-glyceraldehyde + NADPH + H+
-
Bos taurus glycerol + NADP+
-
?
1.1.1.21 L-idose + NADPH + H+
-
Homo sapiens alditol + NADP+
-
?
1.1.1.21 L-idose + NADPH + H+
-
Bos taurus alditol + NADP+
-
?
1.1.1.21 L-threose + NADPH + H+
-
Homo sapiens ?
-
?
1.1.1.21 L-threose + NADPH + H+
-
Bos taurus ?
-
?
1.1.1.21 additional information due to the unavoidable presence of the hemiacetal, glucose reduction by aldose reductase occurs under different conditions with respect to other relevant enzyme substrates, such as alkanals and alkenals, coming from membrane lipid peroxidation Homo sapiens ?
-
?
1.1.1.21 additional information due to the unavoidable presence of the hemiacetal, glucose reduction by aldose reductase occurs under different conditions with respect to other relevant enzyme substrates, such as alkanals and alkenals, coming from membrane lipid peroxidation Bos taurus ?
-
?
1.1.1.21 additional information ability of the enzyme to interact and reduce highly hydrophilic and bulky substrates, substrate specificity an kinetics, overview Homo sapiens ?
-
?
1.1.1.21 additional information ability of the enzyme to interact and reduce highly hydrophilic and bulky substrates, substrate specificity an kinetics, overview Bos taurus ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.21 ? x * 34000, about, SDS-PAGE Homo sapiens
1.1.1.21 ? x * 34000, about, SDS-PAGE Bos taurus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.21 AKR1B1 gene name, UniProt Homo sapiens
1.1.1.21 AKR1B1 gene name, UniProt Bos taurus
1.1.1.21 aldose reductase
-
Homo sapiens
1.1.1.21 aldose reductase
-
Bos taurus
1.1.1.21 BAR
-
Bos taurus
1.1.1.21 HAR
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.21 37
-
assay at Homo sapiens
1.1.1.21 37
-
assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.21 6.8
-
assay at Homo sapiens
1.1.1.21 6.8
-
assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.21 NADPH NADPH-dependent enzyme Homo sapiens
1.1.1.21 NADPH NADPH-dependent enzyme Bos taurus