Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding

Morillas, M, McVey, C E, Brannigan, J A et al. (3 more authors) (2003) Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding. Biochemical journal. pp. 143-150. ISSN 1470-8728

Abstract

Metadata

Item Type: Article
Authors/Creators:
  • Morillas, M
  • McVey, C E
  • Brannigan, J A (jim.brannigan@york.ac.uk)
  • Ladurner, A G
  • Forney, L J
  • Virden, R
Copyright, Publisher and Additional Information:

© 2003 Biochemical Society. Mounted on the Internet with permission from the Biochemical Society 2003.

Keywords: directed evolution,enzyme kinetics,three-dimensional structure,ESCHERICHIA-COLI ATCC-11105,KLUYVERA-CITROPHILA,ACTIVE-SITE,DIRECTED EVOLUTION,CRYSTAL-STRUCTURES,CATALYTIC CENTER,ALKALINE PH,ENZYME,CONFORMATION,EXPRESSION
Dates:
  • Published: 1 April 2003
Institution: The University of York
Academic Units: The University of York > Faculty of Sciences (York) > Chemistry (York)
Depositing User: Sherpa Assistant
Date Deposited: 24 Jun 2005
Last Modified: 16 Oct 2024 11:54
Status: Published
Refereed: Yes
Related URLs:
Open Archives Initiative ID (OAI ID):

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