Steroids and steroidases. IX. Activation parameters and the mechanism of base- and enzyme-catalyzed isomerizations of androst-5-ene-3,17-dione. The nature of the active center of the Δ5 → Δ4-3-ketosteroid isomerase of Pseudomonas testosteroni
1969 ◽
Vol 47
(23)
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pp. 4459-4466
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Keyword(s):
Determination of the activation parameters for the acid-, base-, and enzyme-catalyzed isomerizations of androst-5-ene-3,17-dione has revealed that the facility of the enzymic process is mainly due to an extremely low enthalpy of activation of 5.0 kcal mole−1. Further circumstantial evidence regarding the nature of the reacting groups at the active center has also been obtained, and a mechanism of enzyme action is proposed employing tyrosine and histidine as the principal amino acids responsible for catalyzing the isomerization.
1993 ◽
Vol 58
(16)
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pp. 4487-4489
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1990 ◽
Vol 57
(1)
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pp. 149-150
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Keyword(s):
1998 ◽
Vol 308
◽
pp. 43-53
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2006 ◽
Vol 37
(2)
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pp. 189-201
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2015 ◽
2011 ◽
Vol 29
(3)
◽
pp. 239-243
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1979 ◽
Vol 44
(2)
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pp. 401-405
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