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Literature summary for 1.1.1.62 extracted from

  • Kristan, K.; Deluca, D.; Adamski, J.; Stojan, J.; Rizner, T.L.
    Dimerization and enzymatic activity of fungal 17beta-hydroxysteroid dehydrogenase from the short-chain dehydrogenase/reductase superfamily (2005), BMC Biochem., 6, 28.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain JM107 Curvularia lunata

Protein Variants

Protein Variants Comment Organism
H111A site-directed mutagenesis, the mutant is dimeric like the wild-type enzyme, inactive mutant Curvularia lunata
H111L site-directed mutagenesis, the mutation renders the enzyme monomeric, inactive mutant Curvularia lunata
R129D site-directed mutagenesis, the mutation renders the enzyme monomeric, the mutant shows reduced activity compared to the wild-type enzyme Curvularia lunata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00006
-
NADP+ pH 8.0, 25°C, wild-type enzyme Curvularia lunata
0.0046
-
NADP+ pH 8.0, 25°C, mutant H111A Curvularia lunata
0.0065
-
NADPH pH 8.0, 25°C, wild-type enzyme Curvularia lunata
0.0506
-
NADPH pH 8.0, 25°C, mutant H111A Curvularia lunata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-estrene-3,17-dione + NADPH Curvularia lunata
-
4-estrene-17beta-ol-3-one + NADP+
-
r
estrone + NADPH Curvularia lunata
-
17beta-estradiol + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Curvularia lunata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain JM107 by glutathione affinity chromatography Curvularia lunata

Reaction

Reaction Comment Organism Reaction ID
17beta-estradiol + NAD(P)+ = estrone + NAD(P)H + H+ structure-function analysis, dimerization is crucial for catalytic activity Curvularia lunata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-estrene-3,17-dione + NADPH
-
Curvularia lunata 4-estrene-17beta-ol-3-one + NADP+
-
r
estrone + NADPH
-
Curvularia lunata 17beta-estradiol + NADP+
-
r

Subunits

Subunits Comment Organism
dimer wild-type 17beta-HSD and mutant H111A Curvularia lunata
monomer mutants R129D and H111L, the monomeric enzymes are catalytically inactive Curvularia lunata
More the enzyme functions as dimer or tetramer, but is a dimer under native conditions, secondary structure analysis of wild-type and mutant enzymes, and structure-function analysis, residues involved in dimerization or oligomerization of the enzyme via salt bridges or hydrophobic interactions, overview Curvularia lunata
tetramer
-
Curvularia lunata

Synonyms

Synonyms Comment Organism
17beta-HSD
-
Curvularia lunata
More the enzyme belongs to the short-chain dehydrogenase/reductase superfamily Curvularia lunata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Curvularia lunata

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
denaturation of monomeric enzyme at higher temperatures Curvularia lunata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.65
-
NADP+ pH 8.0, 25°C, wild-type enzyme Curvularia lunata
0.9
-
NADP+ pH 8.0, 25°C, mutant H111A Curvularia lunata
2.4
-
NADPH pH 8.0, 25°C, mutant H111A Curvularia lunata
3.8
-
NADPH pH 8.0, 25°C, wild-type enzyme Curvularia lunata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Curvularia lunata

Cofactor

Cofactor Comment Organism Structure
NADP+ dependent on Curvularia lunata
NADPH dependent on Curvularia lunata