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Literature summary for 1.3.1.3 extracted from

  • Thorn, A.; Egerer-Sieber, C.; Jaeger, C.; Herl, V.; Mueller-Uri, F.; Kreis, W.; Muller, Y.
    The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases (2008), J. Biol. Chem., 283, 17260-17269.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain M15 Digitalis lanata

Crystallization (Commentary)

Crystallization (Comment) Organism
5beta-POR, in the presence and absence of the cofactor NADP+, hanging drop vapour diffusion method, using 15% polyethylene glycol 4000, 0.1 M ammonium acetate, and 0.1 M sodium citrate, pH 5.6 Digitalis lanata

Protein Variants

Protein Variants Comment Organism
Y179A inactive Digitalis lanata
Y179F inactive Digitalis lanata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
progesterone purified wild type enzyme Digitalis lanata

Organism

Organism UniProt Comment Textmining
Digitalis lanata Q6PQJ9
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel-Sepharose affinity column chromatography and Superdex 75 gel filtration Digitalis lanata

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.89
-
purified wild type enzyme, using progesterone as substrate Digitalis lanata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
progesterone + NADPH + H+
-
Digitalis lanata 5beta-pregnane-3,20-dione + NADP+
-
?

Synonyms

Synonyms Comment Organism
5beta-POR
-
Digitalis lanata
progesterone 5beta-reductase
-
Digitalis lanata

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Digitalis lanata