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Literature summary extracted from
- X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP+ and the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (2013), Chem. Biol. Interact., 202, 178-185.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.21 | gene AKR1B1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Homo sapiens |
| 1.1.1.21 | gene AKR1B10, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.1.1.21 | purified recombinant wild-type enzyme and mutant AKR1B10 V301L holoenzyme in complex with inhibitor fidarestat and NADP+, X-ray diffraction structure determination and analysis 1.60 A resolution by replacement soaking of crystals containing inhibitor tolrestat for 14 days in 25 mM fidarestat dissolved in the reservoir solution. For crystallization of the enzyme with tolrestat by hanging-drop vapour diffusion method, 0.001 ml of 18 mg/ml protein solution containing 2 mM tolrestat is mixed with 0.001 ml of reservoir solution containing 100 mM sodium cacodylate, pH 9.0, and 30% v/v PEG, 6000, at 24°C | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.1.21 | V301L | site-directed mutagenesis | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.21 | fidarestat | an inhibitor highly selective for aldose reductase (AKR1B1, EC 1.1.1.21) versus aldehyde reductase (AKR1A1, EC 1.1.1.2). Inhibitor binding site and structure comparisons of enzymes AKR1B1 and AKR1B10, overview. Fidarestat is specific for aldose reductase AKR1B1 versus aldose reductae-like AKR1B10; an inhibitor highly selective for aldose reductase (AKR1B1, EC 1.1.1.21) versus aldehyde reductase (AKR1A1, EC 1.1.1.2). Inhibitor binding site and structure comparisons of enzymes AKR1B1 and AKR1B10, overview. Fidarestat is specific for aldose reductase AKR1B1 versus aldose reductae-like AKR1B10 | Homo sapiens |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.21 | 6 | - |
DL-glyceraldehyde | pH 7.0, 25°C, recombinant detagged enzyme | Homo sapiens | |
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 | - |
sorbitol + NADP+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.21 | Homo sapiens | O60218 | - |
- |
| 1.1.1.21 | Homo sapiens | P15121 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.21 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, followed by anion exchange chromatography | Homo sapiens |
| 1.1.1.21 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, followed by anion exchange chromatography | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.21 | D-glucose + NADPH + H+ | - |
Homo sapiens | sorbitol + NADP+ | - |
? | |
| 1.1.1.21 | DL-glyceraldehyde + NADPH + H+ | - |
Homo sapiens | glycerol + NADP+ | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.21 | AKR1B1 | - |
Homo sapiens |
| 1.1.1.21 | AKR1B10 | - |
Homo sapiens |
| 1.1.1.21 | aldose reductase | - |
Homo sapiens |
| 1.1.1.21 | aldose reductase-like | - |
Homo sapiens |
| 1.1.1.21 | small intestine reductase | - |
Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.21 | 25 | - |
assay at | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.21 | 7 | - |
assay at | Homo sapiens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.21 | NADPH | - |
Homo sapiens | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.21 | 0.000026 | - |
pH 7.0, 25°C, recombinant detagged enzyme | Homo sapiens | fidarestat | |
| 1.1.1.21 | 0.0018 | - |
pH 7.0, 25°C, recombinant detagged enzyme | Homo sapiens | fidarestat | |
| 1.1.1.21 | 0.033 | - |
pH 7.0, 25°C, recombinant detagged wild-type enzyme | Homo sapiens | fidarestat | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.1.1.21 | Homo sapiens | aldose reductase is upregulated in hyperglycemia | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.1.21 | evolution | the enzyme AKR1B1 belongs to the AKR1B subfamily | Homo sapiens |
| 1.1.1.21 | evolution | the enzyme AKR1B10 belongs to the AKR1B subfamily | Homo sapiens |
| 1.1.1.21 | physiological function | AKR1B10 is a tumor marker and displays high activity with the retinoic acid precursor all-trans-retinaldehyde and is induced in different types of cancer, notably in non-small cell lung and hepatocellular carcinomas | Homo sapiens |
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