Literature summary for 1.1.1.50 extracted from

Hoffmann, F.; Sotriffer, C.; Evers, A.; Xiong, G.; Maser, E.
Understanding oligomerization in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: an in silico approach and evidence for an active protein (2007), J. Biotechnol., 129, 131-139.

Search for more literature for 1.1.1.50

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli	Comamonas testosteroni

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of insertion mutants, overview	Comamonas testosteroni

Organism

Organism	UniProt	Comment	Textmining
Comamonas testosteroni	P80702	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography	Comamonas testosteroni

Subunits

Subunits	Comment	Organism
dimer	the dimerization takes place via an interface axis. The formation of a tetramer is blocked in 3alpha-HSD/CR by the presence of a predominantly alpha-helical subdomain which is missing in all other SDRs of known structure, overview	Comamonas testosteroni
More	domain structure, the enzyme possessses a 28 amino acids insertion into the classical Rossmann-fold motif between strand betaE and helix alphaF, preventing the formation of a four helix bundle and enables the dimerization via a P-axis interface, structure homology modelling and simulation, structure comparison, overview	Comamonas testosteroni

Synonyms

Synonyms	Comment	Organism
3alpha-HSD/CR	-	Comamonas testosteroni
More	cf. EC 1.1.1.213, the enzyme belongs to the short chain dehydrogenase/reductase protein superfamily	Comamonas testosteroni

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Release 2023.1 (January 2023)