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

Morillas, M, McVey, C E, Brannigan, J A, Ladurner, A G, Forney, L J and Virden, R (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

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
Institution: The University of York
Academic Units: The University of York > Chemistry (York)
Depositing User: Sherpa Assistant
Date Deposited: 24 Jun 2005
Last Modified: 05 Apr 2016 22:14
Status: Published
Refereed: Yes

Download

Filename: branniganja18.pdf

Description: branniganja18.pdf

Share / Export