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Literature summary for 1.1.1.21 extracted from

  • Brownlee, J.M.; Carlson, E.; Milne, A.C.; Pape, E.; Harrison, D.H.
    Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes (2006), Bioorg. Chem., 34, 424-444.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type enzyme complexed with inhibitors phenylacetic acid, 2-hydroxyphenylacetic acid, 2,6-dichlorophenylacetic acid, hexanoic acid, and lipoic acid, hanging drop vapor diffusion method, 4°C, 23-25 mg/ml protein in 0.10 M sodium phosphate buffer, pH 7.0, mixed with well solution containing 20% w/v PEG 6000 and 50 mM sodium citrate, pH 5.0, microseeding, 1 month, crystal stabilization by 0.1 to 1.0% glutaraldehyde, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
C298A/W219Y site-directed mutagenesis, altered kinetics and thermodynamics in phenylacetic acid derivative inhibitor binding compared to the wild-type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2,6-dichlorophenylacetic acid competitive Homo sapiens
2-bromophenylacetic acid competitive Homo sapiens
2-Chlorophenylacetic acid competitive Homo sapiens
2-hydroxyphenylacetic acid competitive Homo sapiens
2-naphthylacetic acid competitive Homo sapiens
DL-dihydrolipoic acid binds very tight to the enzyme, best inhibitor of the investigated, competitive Homo sapiens
DL-lipoamide binds three-fold more weakly than D,L-lipoic acid, competitive Homo sapiens
DL-lipoic acid is effective in the treatment of diabetic complications, binds tightly to the enzyme, competitive Homo sapiens
hexanoic acid competitive Homo sapiens
Mandelic acid competitive Homo sapiens
additional information enzyme-inhibitor complex structures, the hydrophobic nature of the enzyme active site makes significant contributions to inhibitor binding rather than a reliance on pi-pi orbital interactions with Trp 20, overview Homo sapiens
phenylacetic acid competitive Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35727
-
x * 35727, sequence calculation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyceraldehyde + NADPH + H+
-
Homo sapiens glycerol + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 35727, sequence calculation Homo sapiens

Synonyms

Synonyms Comment Organism
AKR1B1
-
Homo sapiens
aldose reductase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics and thermodynamic studies of inhibitors binding to the enzyme, overview Homo sapiens