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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.50 expression of His-tagged wild-type and mutant enzymes in Escherichia coli Comamonas testosteroni
1.1.1.53 native and insertion protein, expressed as His-tag fusion protein in Escherichia coli XL1-blue and BL21 Comamonas testosteroni
1.1.1.213 expression of His-tagged wild-type and mutant enzymes in Escherichia coli Comamonas testosteroni

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.184 homology modeling of native enzyme, enzyme lacking the extra loop domain, and exchange of the extra loop domain for the short extra loop of 3alpha/20beta-hydroxysteroid dehydrogenase Comamonas testosteroni

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.50 additional information construction of insertion mutants, overview Comamonas testosteroni
1.1.1.184 additional information removal of the extra-loop domain in 3alpha/hydroxysteroid dehydrogenase/carbonyl reductase may lead to the formation of an enzymatically active homotetramer Comamonas testosteroni
1.1.1.213 additional information construction of insertion mutants, overview Comamonas testosteroni

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.53 23380
-
 x * 23380, insertion protein, calculated from the deduced amino acid sequence, confirmed by SDS-PAGE Comamonas testosteroni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.53 additional information Comamonas testosteroni catalyzes the oxidoreduction of a variety of steroid substrates, including the steroid antibiotic fusidic acid, catalyzes the interconversion of hydroxy and oxo groups at position 3 of the steroid ring structure, enzyme is capable of catalyzing the carbonyl reduction of non-steroidal xenobiotic carbonyl compounds, contributes to the bioremediation of natural and synthetic toxicants, plays a central role in steroid metabolism ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.50 Comamonas testosteroni P80702
-
-
1.1.1.53 Comamonas testosteroni
-
 able to use steroids as sole carbon source
-
1.1.1.184 Comamonas testosteroni
-
 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
-
1.1.1.213 Comamonas testosteroni
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.50 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography Comamonas testosteroni
1.1.1.53 recombinant protein using His-tag Comamonas testosteroni
1.1.1.213 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography Comamonas testosteroni

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.53 androstan-3alpha,17beta-diol + NAD+ = 17beta-hydroxyandrostan-3-one + NADH + H+ catalytic residues are Ser114, Tyr127, and Lys131 Comamonas testosteroni
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.53 additional information catalyzes the oxidoreduction of a variety of steroid substrates, including the steroid antibiotic fusidic acid, catalyzes the interconversion of hydroxy and oxo groups at position 3 of the steroid ring structure, enzyme is capable of catalyzing the carbonyl reduction of non-steroidal xenobiotic carbonyl compounds, contributes to the bioremediation of natural and synthetic toxicants, plays a central role in steroid metabolism Comamonas testosteroni ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.50 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
1.1.1.50 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
1.1.1.53 ? x * 23380, insertion protein, calculated from the deduced amino acid sequence, confirmed by SDS-PAGE Comamonas testosteroni
1.1.1.53 dimer crystal structure analysis, in silico data Comamonas testosteroni
1.1.1.184 dimer crystallization data and homology modeling Comamonas testosteroni
1.1.1.213 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
1.1.1.213 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

EC Number Synonyms Comment Organism
1.1.1.50 3alpha-HSD/CR
-
 Comamonas testosteroni
1.1.1.50 More cf. EC 1.1.1.213, the enzyme belongs to the short chain dehydrogenase/reductase protein superfamily Comamonas testosteroni
1.1.1.53 3alpha-HSD/CR
-
 Comamonas testosteroni
1.1.1.53 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase belongs to the short chain dehydrogenase/reductase (SDR) protein superfamily Comamonas testosteroni
1.1.1.213 3alpha-HSD/CR
-
 Comamonas testosteroni
1.1.1.213 More cf. EC 1.1.1.50, the enzyme belongs to the short chain dehydrogenase/reductase protein superfamily Comamonas testosteroni