Journal article
Phospholipase A 1 Activity and Catalytic Mechanism of Pancreatic Cholesterol Esterase
Phosphorus, Sulfur, and Silicon and the Related Elements, Vol.51(1-4), pp.43-46
09/01/1990
DOI: 10.1080/10426509008040678
Abstract
The catalytic mechanism of bovine pancreatic cholesterol esterase (CEase) has been probed by using lipid p-nitrophenyl esters and thiophospholipids as substrates. The rate of CEase-catalyzed hydrolyses of p-nitrophenyl esters is highest for substrates that have fatty acyl chains of intermediate length, while solvent isotope effects decrease with increasing chain length. Nucleophilic trapping experiments indicate that k cat for these substrates is rate limited by hydrolysis of acylenzyme intermediates. The k cat for CEase-catalyzed hydrolysis of 1(3)-decanoylthio-2-decanoyl-phosphatidylcholine is nearly the same as that for p-nitrophenyl decanoate, which demonstrates that phospholipolysis is also rate limited by deacylation. Hence, the CEase and serine protease catalytic mechanisms are similar pro forma . This information is used to guide the design of mechanism-based inhibitors, two classes of which, phosphates and enolphosphates, are described herein.
Details
- Title: Subtitle
- Phospholipase A 1 Activity and Catalytic Mechanism of Pancreatic Cholesterol Esterase
- Creators
- Daniel M Quinn - Department of Chemistry , The University of IowaLarry D Sutton - Department of Chemistry , The University of IowaJay S Stout - Department of Chemistry , The University of IowaTheodora Calogeropoulou - Department of Chemistry , The University of IowaDavid F Wiemer - Department of Chemistry , The University of IowaH. Stewart Hendrickson - Department of Chemistry , St. Olaf College
- Resource Type
- Journal article
- Publication Details
- Phosphorus, Sulfur, and Silicon and the Related Elements, Vol.51(1-4), pp.43-46
- Publisher
- Taylor & Francis Group
- DOI
- 10.1080/10426509008040678
- ISSN
- 1042-6507
- eISSN
- 1563-5325
- Language
- English
- Date published
- 09/01/1990
- Academic Unit
- Chemistry; Neuroscience and Pharmacology
- Record Identifier
- 9983985982302771
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