Determination and use of a transition state for the enzyme estrone sulfatase (ES) from a proposed reaction mechanism.
Using the postulated mechanism for the enzyme estrone sulfatase (ES), we have determined a possible transition state for the reaction catalysed by ES as a representation of the active site. Using the derived structure, we have undertaken the molecular modelling of several steroidal and non-steroidal inhibitors in an attempt to rationalise the inhibitory activity of a number of potent inhibitors.
Ahmed
S
S
School of Chemical and Pharmaceutical Sciences, Kingston University, Penrhyn Road, Kingston upon Thames, Surrey KT1 2EE, UK. s.ahmed@kingston.ac.uk
James
K
K
Owen
C P
CP
Patel
C K
CK
Patel
M B
MB
D020134:Catalytic Domain; D003374:Coumarins / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D004970:Estrone / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology; D020128:Inhibitory Concentration 50; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013429:Sulfatases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D013449:Sulfonamides / Q000494:pharmacology; D013451:Sulfonic Acids
D003374:Coumarins; D004791:Enzyme Inhibitors; D013449:Sulfonamides; D013451:Sulfonic Acids; C088768:estrone-3-O-sulfamate; D004970:Estrone; C520511:irosustat; D013429:Sulfatases; C020121:estrone sulfatase