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Literature summary for 1.1.1.53 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)

Cloned (Comment) Organism
native and insertion protein, expressed as His-tag fusion protein in Escherichia coli XL1-blue and BL21 Comamonas testosteroni

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Comamonas testosteroni
-
able to use steroids as sole carbon source
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein using His-tag Comamonas testosteroni

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits Comment Organism
? x * 23380, insertion protein, calculated from the deduced amino acid sequence, confirmed by SDS-PAGE Comamonas testosteroni
dimer crystal structure analysis, in silico data Comamonas testosteroni

Synonyms

Synonyms Comment Organism
3alpha-HSD/CR
-
Comamonas testosteroni
3alpha-hydroxysteroid dehydrogenase/carbonyl reductase belongs to the short chain dehydrogenase/reductase (SDR) protein superfamily Comamonas testosteroni