Mechanism of the Reaction Catalyzed by .DELTA.5-3-Ketosteroid Isomerase of Comamonas (Pseudomonas) testosteroni: Kinetic Properties of a Modified Enzyme in Which Tyrosine 14 Is Replaced by 3-Fluorotyrosine

Biochemistry ◽  
1994 ◽  
Vol 33 (9) ◽  
pp. 2682-2687 ◽  
Author(s):  
Bob Brooks ◽  
William F. Benisek
Keyword(s):  
Kinetic Properties ◽  
Ketosteroid Isomerase ◽  
Modified Enzyme ◽  
Tyrosine 14 ◽  
Mechanism Of The Reaction ◽  
Pseudomonas Testosteroni

scholarly journals Mass spectrometric studies of a modified active-site tetrapeptide from delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni.

1982 ◽  
Vol 257 (21) ◽  
pp. 12589-12593
Author(s):  
T M Penning ◽  
D N Heller ◽  
T M Balasubramanian ◽  
C C Fenselau ◽  
P Talalay
Keyword(s):  
Active Site ◽  
Mass Spectrometric ◽  
Ketosteroid Isomerase ◽  
Pseudomonas Testosteroni

AFFINITY LABELING OF Δ5 -3-KETOSTEROID ISOMERASE FROM PSEUDOMONAS TESTOSTERONI

1981 ◽  
Vol 9 (2) ◽  
pp. 322P-322P
Author(s):  
Trevor Penning ◽  
Douglas Covey ◽  
Paul Talalay
Keyword(s):  
Affinity Labeling ◽  
Ketosteroid Isomerase ◽  
Pseudomonas Testosteroni

Enzyminduktion mit Steroiden bei Pseudomonas testosteroni

1965 ◽  
Vol 20 (6) ◽  
pp. 547-553 ◽  
Author(s):  
Adolf Wacker ◽  
Jürgen Drews ◽  
William B. Pratt ◽  
Henry Laurent ◽  
Karl Petzoldt
Keyword(s):  
Enzyme Induction ◽  
Selective Inhibition ◽  
Hydroxysteroid Dehydrogenase ◽  
Ketosteroid Isomerase ◽  
Synthetic Pathway ◽  
Induction Process ◽  
Kinetics Of ◽  
Pseudomonas Testosteroni

Steroid initiated enzyme induction (Δ5-Ketosteroid-Isomerase, 3α-Hydroxysteroid-Dehydrogenase, and 3β.17β-Hydroxysteroid-Dehydrogenase) in Pseudomonas testosteroni was investigated with respect to the kinetics of induction, operon control of the induced enzymes, and the relative strengths of various inducers. The induction process was followed indirectly by selective inhibition of different stages in the protein synthetic pathway. Comparisons between bacterial and mammalian steroid induction are discussed.

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