Ij. Kass et Ns. Sampson, THE IMPORTANCE OF GLU(361) POSITION IN THE REACTION CATALYZED BY CHOLESTEROL OXIDASE, Bioorganic & medicinal chemistry letters, 8(19), 1998, pp. 2663-2668
Cholesterol oxidase stereospecifically isomerizes cholest-5-en-3-one t
o cholest-4-en-3-one. When the base catalyst for isomerization, Glu(36
1), is mutated to Asp, the rate of deprotonation of cholest-5-en-3-one
is not affected, but protonation of the dienolic intermediate becomes
rate-limiting. This may be a consequence of the large distance betwee
n the catalytic base and carbon-6 of the intermediate in the mutant en
zyme. (C) 1998 Elsevier Science Ltd. All rights reserved.