Probing the substrate specificity of aminopyrrolnitrin oxygenase (PrnD) by mutational analysis.
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ABSTRACT:
SUBMITTER: Lee JK
PROVIDER: S-EPMC1595372 | biostudies-literature | 2006 Sep
REPOSITORIES: biostudies-literature
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Probing the substrate specificity of aminopyrrolnitrin oxygenase (PrnD) by mutational analysis.
Lee Jung-Kul JK Ang Ee-Lui EL Zhao Huimin H
Journal of bacteriology 20060901 17
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 high ...[more]
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