Appl Environ Microbiol. 2009 May;75(10):3258-62. Epub 2009 Mar 6.

Lateral transfer of genes for hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) degradation.

Andeer PF, Stahl DA, Bruce NC, Strand SE.

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Department of Civil and Environmental Engineering, University of Washington, 201 More Hall, Seattle, WA 98195-2700, USA.

Abstract

Recent studies demonstrated that degradation of the military explosive hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) by species of Rhodococcus, Gordonia, and Williamsia is mediated by a novel cytochrome P450 with a fused flavodoxin reductase domain (XplA) in conjunction with a flavodoxin reductase (XplB). Pulse field gel analysis was used to localize xplA to extrachromosomal elements in a Rhodococcus sp. and distantly related Microbacterium sp. strain MA1. Comparison of Rhodococcus rhodochrous 11Y and Microbacterium plasmid sequences in the vicinity of xplB and xplA showed near identity (6,710 of 6,721 bp). Sequencing of the associated 52.2-kb region of the Microbacterium plasmid pMA1 revealed flanking insertion sequence elements and additional genes implicated in RDX uptake and degradation.

PMID:: 19270122; [PubMed - indexed for MEDLINE]
PMCID:: PMC2681654

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Cited by 2 PubMed Central articles

Functional characterization of pGKT2, a 182-kilobase plasmid containing the xplAB genes, which are involved in the degradation of hexahydro-1,3,5-trinitro-1,3,5-triazine by Gordonia sp. strain KTR9. [Appl Environ Microbiol. 2010]
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The 1.5-A structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive. [J Biol Chem. 2009]
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Sabbadin F, Jackson R, Haider K, Tampi G, Turkenburg JP, Hart S, Bruce NC, Grogan G. J Biol Chem. 2009 Oct 9; 284(41):28467-75. Epub 2009 Aug 19.

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