1 n bond is catalytically relevant in Delta(5)-3-ketosteroid isomerase.

2 ve Y55F/Y88F "Tyr-14-only" mutant of delta 5-3-ketosteroid isomerase complexed with 19-nortestosteron

3                                      Delta 5-3-Ketosteroid isomerase (EC 5.3.3.1) promotes an allylic

4 ide chain resonances of steroid-bound delta5-3-ketosteroid isomerase (EC 5.3.3.1), a homodimeric enzy

5 e, Tyr-14, in free and steroid-bound delta 5-3-ketosteroid isomerase (EC 5.3.3.1, homodimer, M(r) = 2

6                                     Delta(5)-3-ketosteroid isomerase from Pseudomonas putida catalyze

7 ibitors bound at the active site of Delta(5)-3-ketosteroid isomerase from Pseudomonas putida were fou

8 ns of the Y55F/Y88F modified form of Delta 5-3-ketosteroid isomerase in which the active-site tyrosin

9  anesthetic halothane and homodimeric Delta5-3-ketosteroid isomerase (KSI) are characterized by flexi

10               To further understand Delta(5)-3-ketosteroid isomerase (KSI) catalysis, we carried out

11                                     Delta(5)-3-Ketosteroid Isomerase (KSI) catalyzes the isomerizatio

12 site of a highly proficient enzyme, Delta(5)-3-ketosteroid isomerase (KSI), in response to a sudden e

13  allylic rearrangement exemplified by Delta5-3-ketosteroid isomerase (KSI; EC 5.3.3.1).

14     3-Oxo-Delta 5-steroid isomerase (Delta 5-3-ketosteroid isomerase, KSI; EC 5.3.3.1) catalyzes the

15 d equilenin show the active site of Delta(5)-3-ketosteroid isomerase to be largely unperturbed by the

16 ole in the active site of wild-type Delta(5)-3-ketosteroid isomerase to have a proton affinity equal

17 mic the catalytic reaction cycle of Delta(5)-3-ketosteroid isomerase to probe the functionally releva