ArticleJournal of bacteriology2006
Probing the substrate specificity of aminopyrrolnitrin oxygenase (PrnD) by mutational analysis.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Fermentative aminopyrrolnitrin production by metabolically engineered Corynebacterium glutamicum.Microbial cell factories · 2024Article
- Engineering Rieske oxygenase activity one piece at a time.Current opinion in chemical biology · 2023Review
- Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Chemical reviews · 2017Review
- Mechanism and Catalytic Diversity of Rieske Non-Heme Iron-Dependent Oxygenases.ACS catalysis · 2013Article
- From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes.International journal of molecular sciences · 2013Review
- The ternary complex of PrnB (the second enzyme in the pyrrolnitrin biosynthesis pathway), tryptophan, and cyanide yields new mechanistic insights into the indolamine dioxygenase superfamily.The Journal of biological chemistry · 2010Article
- Nitroaromatic compounds, from synthesis to biodegradation.Microbiology and molecular biology reviews : MMBR · 2010Review
- Diversity of cultivated endophytic bacteria from sugarcane: genetic and biochemical characterization of Burkholderia cepacia complex isolates.Applied and environmental microbiology · 2007Article
- The second enzyme in pyrrolnitrin biosynthetic pathway is related to the heme-dependent dioxygenase superfamily.Biochemistry · 2007Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.