Probing the substrate specificity of aminopyrrolnitrin oxygenase (PrnD) by mutational analysis

Jung Kul Lee, Ee Lui Ang, Huimin Zhao

Research output: Contribution to journalArticlepeer-review

Abstract

Molecular modeling and mutational analysis (site-directed mutagenesis and saturation mutagenesis) were used to probe the molecular determinants of the substrate specificity of aminopyrrolnitrin oxygenase (PrnD) from Pseudomonas fluorescens Pf-5. There are 17 putative substrate-contacting residues, and mutations at two of the positions, positions 312 and 277, could modulate the enzyme substrate specificity separately or in combination. Interestingly, several of the mutants obtained exhibited higher catalytic efficiency (approximately two- to sevenfold higher) with the physiological substrate aminopyrrolnitrin than the wild-type enzyme exhibited.

Original languageEnglish (US)
Pages (from-to)6179-6183
Number of pages5
JournalJournal of bacteriology
Volume188
Issue number17
DOIs
StatePublished - Sep 2006

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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