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Literature summary for 1.1.1.184 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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
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3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
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Subunits

Subunits Comment Organism
dimer crystallization data and homology modeling Comamonas testosteroni