Literature summary 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.

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.3.1.3	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

EC Number	Protein Variants	Comment	Organism
1.3.1.3	Y179A	inactive	Digitalis lanata
1.3.1.3	Y179F	inactive	Digitalis lanata

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.3.1.3	0.12	-	progesterone	purified wild type enzyme	Digitalis lanata

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.3.1.3	Digitalis lanata	Q6PQJ9	-	-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.3.1.3	1.89	-	purified wild type enzyme, using progesterone as substrate	Digitalis lanata

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
1.3.1.3	5beta-POR	-	Digitalis lanata
1.3.1.3	progesterone 5beta-reductase	-	Digitalis lanata

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.3.1.3	NADPH	-	Digitalis lanata

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Release 2023.1 (January 2023)