Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics.

Applied and environmental microbiology - 1 Jun 2006

Leungsakul Thammajun, Johnson Glenn R, Wood Thomas K

Abstract excerpt

4-Methyl-5-nitrocatechol (4M5NC) monooxygenase (DntB) from Burkholderia sp. strain DNT catalyzes the second step of 2,4-dinitrotoluene degradation by converting 4M5NC to 2-hydroxy-5-methylquinone with the concomitant removal of the nitro group. DntB is a flavoprotein that has a very narrow substrate range. Here, error-prone PCR was used to create variant DntB M22L/L380I, which accepts the two new substrates...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biodegradation, Environmental
Share to Burkholderia

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA Primers

Share to Mixed Function Oxygenases

Share to Nitrites

Share to Nitrophenols

Share to Protein Engineering

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 16751499
DOI: 10.1128/AEM.02966-05
PMCID: PMC1489588

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics.PMID 16751499Read ↗

Cloning of Two Gene Clusters Involved in the Catabolism of 2,4-Dinitrophenol by <i>Paraburkholderia</i> sp. Strain KU-46 and Characterization of the Initial DnpAB Enzymes and a Two-Component Monooxygenase DnpC1C2Semantic proximity Read ↗

Oxidation of aminonitrotoluenes by 2,4-DNT dioxygenase of Burkholderia sp. strain DNT.Semantic proximity Read ↗

Controlling the regiospecific oxidation of aromatics via active site engineering of toluene para-monooxygenase of Ralstonia pickettii PKO1.Semantic proximity Read ↗

Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase.Semantic proximity Read ↗

Characterization of a pseudomonad 2-nitrobenzoate nitroreductase and its catabolic pathway-associated 2-hydroxylaminobenzoate mutase and a chemoreceptor involved in 2-nitrobenzoate chemotaxis.Semantic proximity Read ↗

Single Amino Acid Switch between a Flavin-Dependent Dehalogenase and Nitroreductase.Semantic proximity Read ↗

Changing the substrate reactivity of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica HBP1 by directed evolution.Semantic proximity Read ↗

Cloning and characterization of Pseudomonas sp. strain DNT genes for 2,4-dinitrotoluene degradation.Semantic proximity Read ↗

Selection for growth on 3-nitrotoluene by 2-nitrotoluene-utilizing Acidovorax sp. strain JS42 identifies nitroarene dioxygenases with altered specificities.Semantic proximity Read ↗

Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzeri OX1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol.Semantic proximity Read ↗

The Crystal Structure of Engineered Nitroreductase NTR 2.0 and Impact of F70A and F108Y Mutations on Substrate SpecificitySemantic proximity Read ↗

Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.