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Literature summary extracted from

  • Bauer, P.; Rudolph, K.; Mueller-Uri, F.; Kreis, W.
    Vein patterning 1-encoded progesterone 5beta-reductase: activity-guided improvement of catalytic efficiency (2012), Phytochemistry, 77, 53-59.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.3 DNA and amino acid sequence determination and analysis, sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli strain M15 Digitalis lanata
1.3.1.3 DNA and amino acid sequence determination and analysis, sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli strain M15 Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.3 recombinant wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography Digitalis lanata

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.3 C352G site-directed mutagenesis, mutation at the substrate binding site, the mutant shows reduced activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 D181T/L182Q site-directed mutagenesis, mutation at motif V, the mutant shows reduced activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 F353M site-directed mutagenesis, mutation at the substrate binding site, the mutant shows similar activity as the wild-type enzyme Digitalis lanata
1.3.1.3 F353P site-directed mutagenesis, mutation at the substrate binding site, the mutant shows similar activity as the wild-type enzyme Digitalis lanata
1.3.1.3 G204N site-directed mutagenesis, mutation at motif IV, the mutant shows reduced activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 L182Q site-directed mutagenesis, mutation at motif V, the mutant shows similar activity as the wild-type enzyme Digitalis lanata
1.3.1.3 M150L site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme Digitalis lanata
1.3.1.3 N205A site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 N205M site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 N205M/Y156V site-directed mutagenesis, double mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 R146T site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme Digitalis lanata
1.3.1.3 S248M site-directed mutagenesis, mutation near the substrate binding site, inactive mutant Digitalis lanata
1.3.1.3 T65P site-directed mutagenesis, mutation at near motif II, the mutant shows similar activity as the wild-type enzyme Digitalis lanata
1.3.1.3 Y156V site-directed mutagenesis, mutation at the substrate binding site, the mutant shows increased activity compared to the wild-type enzyme Digitalis lanata
1.3.1.3 Y302F site-directed mutagenesis, mutation at motif IV, the mutant shows similar activity as the wild-type enzyme Digitalis lanata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.3 0.063
-
 progesterone pH 8.0, 40°C, recombinant mutant N205M Digitalis lanata
1.3.1.3 0.072
-
 progesterone pH 8.0, 40°C, recombinant mutant Y156V Digitalis lanata
1.3.1.3 0.085
-
 progesterone pH 8.0, 40°C, recombinant mutant N205A Digitalis lanata
1.3.1.3 0.09
-
 progesterone pH 8.0, 40°C, recombinant mutant Y156V/N205M Digitalis lanata
1.3.1.3 0.116
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant wild-type enzyme Arabidopsis thaliana
1.3.1.3 0.175
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant N205A Digitalis lanata
1.3.1.3 0.196
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant N205M Digitalis lanata
1.3.1.3 0.268
-
 progesterone pH 8.0, 40°C, recombinant wild-type enzyme Arabidopsis thaliana
1.3.1.3 0.333
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant wild-type enzyme Digitalis lanata
1.3.1.3 0.334
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant Y156V/N205M Digitalis lanata
1.3.1.3 0.362
-
 progesterone pH 8.0, 40°C, recombinant wild-type enzyme Digitalis lanata
1.3.1.3 1.15
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant Y156V Digitalis lanata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.3 2-cyclohexen-1-one + NADPH + H+ Digitalis lanata
-
 cyclohexanone + NADP+
-
 ?
1.3.1.3 2-cyclohexen-1-one + NADPH + H+ Arabidopsis thaliana
-
 cyclohexanone + NADP+
-
 ?
1.3.1.3 progesterone + NADPH + H+ Digitalis lanata
-
 5beta-pregnane-3,20-dione + NADP+
-
 ?
1.3.1.3 progesterone + NADPH + H+ Arabidopsis thaliana
-
 5beta-pregnane-3,20-dione + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.3 Arabidopsis thaliana Q9STX2
-
-
1.3.1.3 Digitalis lanata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.3 recombinant wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.3 2-cyclohexen-1-one + NADPH + H+
-
 Digitalis lanata cyclohexanone + NADP+
-
 ?
1.3.1.3 2-cyclohexen-1-one + NADPH + H+
-
 Arabidopsis thaliana cyclohexanone + NADP+
-
 ?
1.3.1.3 progesterone + NADPH + H+
-
 Digitalis lanata 5beta-pregnane-3,20-dione + NADP+
-
 ?
1.3.1.3 progesterone + NADPH + H+
-
 Arabidopsis thaliana 5beta-pregnane-3,20-dione + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.3 P5betaR
-
 Digitalis lanata
1.3.1.3 P5betaR
-
 Arabidopsis thaliana
1.3.1.3 progesterone 5beta-reductase
-
 Digitalis lanata
1.3.1.3 progesterone 5beta-reductase
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.1.3 40
-
 assay at Digitalis lanata
1.3.1.3 40
-
 assay at Arabidopsis thaliana

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.3 0.0075
-
 progesterone pH 8.0, 40°C, recombinant mutant Y156V Digitalis lanata
1.3.1.3 0.011
-
 progesterone pH 8.0, 40°C, recombinant mutant Y156V/N205M Digitalis lanata
1.3.1.3 0.019
-
 progesterone pH 8.0, 40°C, recombinant wild-type enzyme Digitalis lanata
1.3.1.3 0.03
-
 progesterone pH 8.0, 40°C, recombinant mutant N205M Digitalis lanata
1.3.1.3 0.037
-
 progesterone pH 8.0, 40°C, recombinant mutant N205A Digitalis lanata
1.3.1.3 0.17
-
 progesterone pH 8.0, 40°C, recombinant wild-type enzyme Arabidopsis thaliana
1.3.1.3 0.4
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant Y156V/N205M Digitalis lanata
1.3.1.3 0.475
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant N205M Digitalis lanata
1.3.1.3 0.49
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant wild-type enzyme Digitalis lanata
1.3.1.3 0.68
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant Y156V Digitalis lanata
1.3.1.3 1.1
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant N205A Digitalis lanata
1.3.1.3 1.11
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant wild-type enzyme Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.3 8
-
 assay at Digitalis lanata
1.3.1.3 8
-
 assay at Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.3 NADPH
-
 Digitalis lanata
1.3.1.3 NADPH
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
1.3.1.3 evolution the enzyme belongs to the aldo–keto reductase (AKR) family, sequence comparisons, overview Digitalis lanata
1.3.1.3 evolution the enzyme belongs to the aldo–keto reductase (AKR) family, sequence comparisons, overview Arabidopsis thaliana
1.3.1.3 additional information residues Tyr156, Asp205, and Ser248 are responsible for the low catalytic efficiency of the enzyme, substrate binding pocket structure, overview Digitalis lanata
1.3.1.3 additional information the enzyme shows high catalytic efficiency Arabidopsis thaliana

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.1.3 0.052
-
 progesterone pH 8.0, 40°C, recombinant wild-type enzyme Digitalis lanata
1.3.1.3 0.105
-
 progesterone pH 8.0, 40°C, recombinant mutant Y156V Digitalis lanata
1.3.1.3 0.122
-
 progesterone pH 8.0, 40°C, recombinant mutant Y156V/N205M Digitalis lanata
1.3.1.3 0.432
-
 progesterone pH 8.0, 40°C, recombinant mutant N205A Digitalis lanata
1.3.1.3 0.473
-
 progesterone pH 8.0, 40°C, recombinant mutant N205M Digitalis lanata
1.3.1.3 0.588
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant Y156V Digitalis lanata
1.3.1.3 0.628
-
 progesterone pH 8.0, 40°C, recombinant wild-type enzyme Arabidopsis thaliana
1.3.1.3 1.19
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant Y156V/N205M Digitalis lanata
1.3.1.3 1.464
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant wild-type enzyme Digitalis lanata
1.3.1.3 2.425
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant N205M Digitalis lanata
1.3.1.3 6.266
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant mutant N205A Digitalis lanata
1.3.1.3 9.607
-
 2-cyclohexen-1-one pH 8.0, 40°C, recombinant wild-type enzyme Arabidopsis thaliana