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Applied and Environmental Microbiology, November 2008, p. 6631-6638, Vol. 74, No. 21
0099-2240/08/$08.00+0     doi:10.1128/AEM.01192-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Involvement of a Novel Enzyme, MdpA, in Methyl tert-Butyl Ether Degradation in Methylibium petroleiphilum PM1 {triangledown}

Radomir Schmidt,1* Vince Battaglia,1 Kate Scow,1 Staci Kane,2 and Krassimira R. Hristova1

Department of Land, Air and Water Resources, University of California, Davis, California,1 Lawrence Livermore National Laboratory, Livermore, California2

Received 28 May 2008/ Accepted 7 September 2008

Methylibium petroleiphilum PM1 is a well-characterized environmental strain capable of complete metabolism of the fuel oxygenate methyl tert-butyl ether (MTBE). Using a molecular genetic system which we established to study MTBE metabolism by PM1, we demonstrated that the enzyme MdpA is involved in MTBE removal, based on insertional inactivation and complementation studies. MdpA is constitutively expressed at low levels but is strongly induced by MTBE. MdpA is also involved in the regulation of tert-butyl alcohol (TBA) removal under certain conditions but is not directly responsible for TBA degradation. Phylogenetic comparison of MdpA to related enzymes indicates close homology to the short-chain hydrolyzing alkane hydroxylases (AH1), a group that appears to be a distinct subfamily of the AHs. The unique, substrate-size-determining residue Thr59 distinguishes MdpA from the AH1 subfamily as well as from AlkB enzymes linked to MTBE degradation in Mycobacterium austroafricanum.

* Corresponding author. Mailing address: Department of Land, Air and Water Resources, University of California, Davis, One Shields Ave., Davis, CA 95616. Phone: (530) 752-1488. Fax: (530) 752-1552. E-mail: radschmidt{at}ucdavis.edu

{triangledown} Published ahead of print on 12 September 2008.

Applied and Environmental Microbiology, November 2008, p. 6631-6638, Vol. 74, No. 21
0099-2240/08/$08.00+0     doi:10.1128/AEM.01192-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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