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National Institute of Environmental Health Sciences

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Your Environment. Your Health.

Publication Detail

Title: Involvement of a novel enzyme, MdpA, in methyl tert-butyl ether degradation in Methylibium petroleiphilum PM1.

Authors: Schmidt, Radomir; Battaglia, Vince; Scow, Kate; Kane, Staci; Hristova, Krassimira R

Published In Appl Environ Microbiol, (2008 Nov)

Abstract: 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 Thr(59) distinguishes MdpA from the AH1 subfamily as well as from AlkB enzymes linked to MTBE degradation in Mycobacterium austroafricanum.

PubMed ID: 18791002 Exiting the NIEHS site

MeSH Terms: Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism*; Betaproteobacteria/enzymology*; Betaproteobacteria/genetics; Biodegradation, Environmental*; Enzymes/genetics; Enzymes/metabolism*; Gene Deletion; Gene Order; Genetic Complementation Test; Methyl Ethers/metabolism*; Molecular Sequence Data; Mutagenesis, Insertional; Phylogeny; Sequence Alignment; Sequence Homology, Amino Acid; tert-Butyl Alcohol/metabolism

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