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Figure 1.
Fig. 1. Dimeric structure, enzymatic reaction mechanism,
and competitive inhibitors of PI. a, the dimeric structure of
KSI in complex with equilenin is shown with the three critical
active site residues and equilenin in a ball-and-stick model. b,
the enzyme mechanism of KSI proceeding through a dienolic
intermediate is shown with the catalytic residues. The H-bond
between the Tyr14 OH and the oxyanion of the intermediate is
indicated in a conventional way to denote a LBHB formation, the
proton being in the middle of the two heavy atoms. c, the three
competitive inhibitors used in this study are shown along with
their markedly different pK[a] values.
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