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Literature summary for 1.1.1.50 extracted from

  • Hwang, C.C.; Chang, P.R.; Hsieh, C.L.; Chou, Y.H.; Wang, T.P.
    Thermodynamic analysis of remote substrate binding energy in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase catalysis (2019), Chem. Biol. Interact., 302, 183-189 .
    View publication on PubMed
Search for more literature for 1.1.1.50

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Comamonas testosteroni
overexpression in Escherichia coli Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni P80702
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-decalol + NAD+
-
 Comamonas testosteroni ? + NADH + H+
-
 ?
androsterone + NAD+ the enzyme uses remote binding interactions to accelerate the reaction of androsterone with NAD+. The remote non-reacting sites of androsterone may induce a conformational change of the substrate binding loop with an entropic cost for better interaction with the transition state to decrease the enthalpy of activation, significantly increasing catalytic efficiency Comamonas testosteroni androstanedione + NADH + H+
-
 ?
androsterone + NAD+ thermodynamic analysis of remote substrate binding energy. The remote non-reacting sites of androsterone may induce a conformational change of the substrate binding loop with an entropic cost for better interaction with the transition state to decrease the enthalpy of activation, significantly increasing catalytic efficiency Comamonas testosteroni androstanedione + NADH + H+
-
 ?
cyclohexanol + NAD+
-
 Comamonas testosteroni ? + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
3alpha-HSD/CR
-
 Comamonas testosteroni
3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
-
 Comamonas testosteroni