The enzyme, characterized from the bacterium Nocardioides sp. JS1661, is involved in the degradation of 2,4-dinitroanisole. Unlike other known O-demethylases, such as EC 1.14.99.15, 4-methoxybenzoate monooxygenase (O-demethylating), or EC 1.14.11.32, codeine 3-O-demethylase, it does not require oxygen or electron donors, and produces methanol rather than formaldehyde.
The expected taxonomic range for this enzyme is: unclassified Nocardioides
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SYSTEMATIC NAME
IUBMB Comments
2,4-dinitroanisole methanol hydrolase
The enzyme, characterized from the bacterium Nocardioides sp. JS1661, is involved in the degradation of 2,4-dinitroanisole. Unlike other known O-demethylases, such as EC 1.14.99.15, 4-methoxybenzoate monooxygenase (O-demethylating), or EC 1.14.11.32, codeine 3-O-demethylase, it does not require oxygen or electron donors, and produces methanol rather than formaldehyde.
Substrates: alkaline hydrolysis of DNAN is associated with considerable C and N isotope fractionation, isotopic analyses by gas chromatography and isotope ratio mass spectrometry (GC/IRMS). Carbon and nitrogen isotope enrichment factors (epsilonC and epsilonN), apparent 13C and 15N kinetic isotope effects, and correlations of C and N isotope fractionation (DELTAN/C) associated with the alkaline and enzymatic hydrolysis of DNAN, overview Products: -
evaluation of the C and N isotope fractionation associated with abiotic and biological 2,4-dinitroanisole (DNAN) hydrolysis through alkaline hydrolysis at high pH as well as enzymatic hydrolysis by Nocardioides sp. JS1661 and partially purified DNAN O-demethylase for decontamination of DNAN. Whereas both reactions generate 2,4-dinitrophenol (DNP), compound-specific isotope analysis (CSIA) of DNAN and DNP reveal that these reactions occur by different mechanisms, thus different mechanisms of alkaline and enzymatic hydrolysis of the insensitive munition component 2,4-dinitroanisole lead to identical products
enzyme immobilization by biogenic silica encapsulation which is used to stabilize the enzyme and to enable it to be packed into a model microcolumn for application as a biosensor or as a bioreactor for continuous destruction of 2,4-dinitroanisole (DNAN). The immobilized enzyme is stable and not inhibited by other insensitive munitions constituents. The highly specific, convenient and robust biocatalyst DNAN demethylase can mineralize DNAN. An alternative method for DNAN detection involved coating the encapsulated enzyme on cellulose filter paper. Methods, detailed overview
the immobilized enzyme can be used as biocatalyst for detection and destruction of the insensitive explosive, 2,4-dinitroanisole (DNAN), with a wide spectrum of applications ranging from national security and demilitarization to environmental monitoring and restoration
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