Substrate spectrum extension of PenA in Burkholderia thailandensis with a single amino acid deletion, Glu168del

Hyojeong Yi, Karan Kim, Kwang Hwi Cho, Oksung Jung, Heenam Kim

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

We describe a deletion mutation in a class A β-lactamase, PenA, of Burkholderia thailandensis that extended the substrate spectrum of the enzyme to include ceftazidime. Glu168del was located in a functional domain called the omega loop causing expansion of the space in the loop, which in turn increased flexibility at the active site. This deletion mutation represents a rare but significant alternative mechanical path to substrate spectrum extension in PenA besides more common substitution mutations.

Original languageEnglish
Pages (from-to)4005-4008
Number of pages4
JournalAntimicrobial Agents and Chemotherapy
Volume56
Issue number7
DOIs
Publication statusPublished - 2012 Jul 1

Fingerprint

Burkholderia
Sequence Deletion
Amino Acids
Ceftazidime
Catalytic Domain
Mutation
Enzymes

ASJC Scopus subject areas

  • Pharmacology (medical)
  • Pharmacology
  • Infectious Diseases

Cite this

Substrate spectrum extension of PenA in Burkholderia thailandensis with a single amino acid deletion, Glu168del. / Yi, Hyojeong; Kim, Karan; Cho, Kwang Hwi; Jung, Oksung; Kim, Heenam.

In: Antimicrobial Agents and Chemotherapy, Vol. 56, No. 7, 01.07.2012, p. 4005-4008.

Research output: Contribution to journalArticle

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