An esterase with ?-lactamase activity

Jones, Mark and Page, Michael I. (1991) An esterase with ?-lactamase activity. Chemical Communications (5). pp. 316-317. ISSN 1359-7345

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Abstract

Porcine liver esterase selectively catalyses the hydrolysis of the -lactam of the methyl ester of benzylpenicillin with a Kcat/Km of 675 dm3 mol–1 s–1 and without hydrolysing the methyl ester function.

Information

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

URI:

https://eprints.hud.ac.uk/id/eprint/6117

Title:

An esterase with ?-lactamase activity

Creators:

Jones, Mark and Page, Michael I.

Identification Number:

10.1039/C39910000316

Official URL:

http://dx.doi.org/10.1039/C39910000316

Date:

March 1991

Subjects:

Q Science > Q Science (General)
Q Science > QD Chemistry

Schools:

School of Applied Sciences

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Item Type:

Article

Depositing User:

Sharon Beastall

Date Deposited:

06 Nov 2009 10:00

Revision:

Last Modified:

28 Aug 2021 10:52

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