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Title: Enzymatic function in crystals of. delta. /sup 5/-3-ketosteroid isomerase: catalytic activity and binding of competitive inhibitors

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:5132771

Crystals of the steroid-metabolizing enzyme, ..delta../sup 5/-3-ketosteroid isomerase (EC 5.3.3.1) from Pseudomonas testosteroni, exhibit many enzymatic properties. Each enzyme subunit in the lattice binds a competitive inhibitor, progesterone, with the same stoichiometry (1:1) and affinity (K/sub D/ = 6 x 10/sup -6/ M) as the enzyme in solution. Another competitive inhibitor, 19-nortestosterone, competes with progesterone for the same binding sites in the crystal. The enzyme crystals catalyze the conversion of ..delta../sup 5/- to ..delta../sup 4/-ketosteroids, but because the enzyme is so efficient, and substrate diffusion into the crystal is so slow, substrate cannot penetrate deeply into the crystal before being converted to product. A general theoretical formulation is presented to account for the effects of substrate diffusion into enzyme crystals of different shapes and sizes. The dependence of apparent mean enzyme activity in steroid isomerase crystals as a function of crystal size is shown to be consistent with this theoretical formulation. These inhibitor binding and catalytic properties suggest that the enzyme is in an active conformation within these crystals.

Research Organization:
Univ. of Chicago, IL
OSTI ID:
5132771
Journal Information:
J. Biol. Chem.; (United States), Vol. 259:14
Country of Publication:
United States
Language:
English