Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolyses of asymmetric synthetic value

Published

Journal Article

The stereospecificities of the isozyme components of commercially available pig liver esterase have been shown to be essentially the same toward representative monocyclic and acyclic diester substrates. This removes previous concerns that the isozymal composition of pig liver esterase, a widely used catalyst for chiral synthon production, might result in its not behaving consistently when applied as a catalyst for asymmetric synthetic purposes. The results establish that commercial pig liver esterase can be exploited synthetically as a chiral catalyst with confidence that it will behave as if it were a single protein. © 1988, American Chemical Society. All rights reserved.

Full Text

Duke Authors

Cited Authors

  • Lam, LKP; Brown, CM; Lym, L; Toone, EJ; Jones, JB; Jeso, BD

Published Date

  • January 1, 1988

Published In

Volume / Issue

  • 110 / 13

Start / End Page

  • 4409 - 4411

Electronic International Standard Serial Number (EISSN)

  • 1520-5126

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja00221a049

Citation Source

  • Scopus