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J. Biol. Chem., Vol. 266, Issue 7, 4033-4036, 03, 1991
LP DiPersio, RN Fontaine and DY Hui
The histidine residue essential for the catalytic activity of pancreatic
cholesterol esterase (carboxylester lipase) has been identified in this
study using sequence comparison and site-specific mutagenesis techniques.
In the first approach, comparison of the primary structure of rat
pancreatic cholesterol esterase with that of acetylcholinesterase and
cholinesterase revealed two conserved histidine residues located at
positions 420 and 435. The sequence in the region around histidine 420 is
quite different between the three enzymes. However, histidine 435 is
located in a 22-amino acid domain that is 47% homologous with other serine
esterases. Based on this sequence homology, it was hypothesized that
histidine 435 is the histidine residue essential for catalytic activity of
cholesterol esterase. The role of His435 in the catalytic activity of
pancreatic cholesterol esterase was then studied by the site-specific
mutagenesis technique. Substitution of the histidine in position 435 with
glutamine, arginine, alanine, serine, or aspartic acid abolished the
ability of cholesterol esterase to hydrolyze p-nitrophenyl butyrate and
cholesterol [14C]oleate. In contrast, mutagenesis of the histidine residue
at position 420 to glutamine had no effect on cholesterol esterase enzyme
activity. The results of this study strongly suggested that histidine 435
may be a component of the catalytic triad of pancreatic cholesterol
esterase.
Site-specific mutagenesis of an essential histidine residue in pancreatic cholesterol esterase
Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, Ohio 45267-0529.
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