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Literature summary extracted from

  • Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison, D.H.
    The structure of Apo R268A human aldose reductase: Hinges and latches that control the kinetic mechanism (2005), Biochim. Biophys. Acta, 1748, 201-212.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.21 purified recombinant R268A mutant enzyme, hanging drop vapour diffusion method, 30 mg/ml protein in 5 mM phosphate, pH 7.0, mixing with equal volume of well solution containing 20% v/v PEG 6000, 25 mM MES, pH 6.0, and 16 mM ammonium sulfate, 3 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.21 C298A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 G213P site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 G213S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 additional information construction of deletion mutant DELTA214-219 showing reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 R268A site-directed mutagenesis, the mutant shows similar kinetics for the aldehyde substrate, but highly reduced affinity for the nucleotide cofactor, and reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 R293A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 S210A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 S214A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 S226A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 W219A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.1.1.21 W219E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.21 0.02
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant wild-type enzyme Homo sapiens
1.1.1.21 0.02
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant R293A Homo sapiens
1.1.1.21 0.02
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant W219A Homo sapiens
1.1.1.21 0.02
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant W219E Homo sapiens
1.1.1.21 0.03
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant S226A Homo sapiens
1.1.1.21 0.05
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant R268A Homo sapiens
1.1.1.21 0.11
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant S210A Homo sapiens
1.1.1.21 0.13
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant S214A Homo sapiens
1.1.1.21 0.42
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant G213S Homo sapiens
1.1.1.21 0.5
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant DELTA214-219 Homo sapiens
1.1.1.21 0.6
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant C298A Homo sapiens
1.1.1.21 3.7
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant G213P 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 aldose + NADPH + H+ Homo sapiens
-
alditol + NADP+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.21 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.21 recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.21 alditol + NAD(P)+ = aldose + NAD(P)H + H+ the ordered bi-bi kinetic mechanism is controlled by hinges and latches of enzyme structure, residues R268, G213, and S226 are involved Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.21 aldose + NADPH + H+
-
Homo sapiens alditol + NADP+
-
?
1.1.1.21 DL-glyceraldehyde + NADPH + H+
-
Homo sapiens glycerol + NADP+
-
r

Subunits

EC Number Subunits Comment Organism
1.1.1.21 More the cofactor binding loop structure influences the kinetic mechanism of the enzyme, loop movement, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.1.1.21 AKR1B1
-
Homo sapiens
1.1.1.21 aldose reductase
-
Homo sapiens
1.1.1.21 More the enzyme is a member of the aldo-keto reductase family 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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.21 0.09
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant W219E Homo sapiens
1.1.1.21 0.16
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant R293A Homo sapiens
1.1.1.21 0.32
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant W219A Homo sapiens
1.1.1.21 0.38
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant R268A Homo sapiens
1.1.1.21 0.5
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant wild-type enzyme Homo sapiens
1.1.1.21 0.54
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant S226A Homo sapiens
1.1.1.21 2
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant S210A Homo sapiens
1.1.1.21 2.1
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant S214A Homo sapiens
1.1.1.21 2.15
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant DELTA214-219 Homo sapiens
1.1.1.21 3.7
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant G213S Homo sapiens
1.1.1.21 4
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant C298A Homo sapiens
1.1.1.21 4.6
-
DL-glyceraldehyde pH 7.0, 25°C, recombinant mutant G213P 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 dependent on, several factors act to stabilize the NADPH-holding loop in either the open or closed conformation, residues R268, G213, and S226 are involved, loop movement, overview Homo sapiens