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

Morillas, M, McVey, C E, Brannigan, J A orcid.org/0000-0001-6597-8972 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

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Item Type: Article
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© 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: 28 Jun 2025 23:05
Status: Published
Refereed: Yes
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