volume 79, issue 5, P1555-1562 2012
DOI: 10.1128/aem.03215-12
View full text
|
|
Share

Abstract: A homologue of the Escherichia coli penicillin acylase is encoded in the genomes of several thermophiles, including in different Thermus thermophilus strains. Although the natural substrate of this enzyme is not known, this acylase shows a marked preference for penicillin K over penicillin G. Three-dimensional models were created in which the catalytic residues and the substrate binding pocket were identified. Through rational redesign, residues were replaced to mimic the aromatic binding site of the E. coli …

Expand abstract

Search citation statements

Order By: Relevance

Citation Types

0
12
0

Paper Sections

0
0
0
0
0

Publication Types

0
0
0
0

Relationship

0
0

Authors

Journals