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Applied and Environmental Microbiology, July 2008, p. 4028-4035, Vol. 74, No. 13
0099-2240/08/$08.00+0     doi:10.1128/AEM.00422-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Novel Pathway for Catabolism of the Organic Sulfur Compound 3,3'-Dithiodipropionic Acid via 3-Mercaptopropionic Acid and 3-Sulfinopropionic Acid to Propionyl-Coenzyme A by the Aerobic Bacterium Tetrathiobacter mimigardefordensis Strain DPN7{triangledown}

Jan Hendrik Wübbeler, Nadine Bruland, Kornelia Kretschmer, and Alexander Steinbüchel*

Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, 48149 Münster, Germany

Received 20 February 2008/ Accepted 25 April 2008

The hitherto unstudied microbial degradation of the organic disulfide 3,3'-dithiodipropionic acid (DTDP) was investigated with the recently described bacterium Tetrathiobacter mimigardefordensis strain DPN7T (DSM 17166T; LMG 22922T), which is able to use DTDP as the sole carbon source for growth. 3-Mercaptopropionic acid (3MP) and 3-sulfinopropionic acid (3SP) were detected in the growth medium and occurred as intermediates during DTDP degradation. To identify genes coding for enzymes of DTDP catabolism, Tn5::mob-induced mutants of T. mimigardefordensis were generated. Screening of transposon mutant libraries yielded many mutants fully or partially impaired in utilizing DTDP as a carbon source. Mapping of the insertion loci in some mutants identified four disrupted open reading frames (ORFs) with putative metabolic functions. The ORFs were assigned function on the basis of homologies with lpdA (EC 1.8.1.4), cdo (EC 1.13.11.20), sucCD (EC 6.2.1.5), and acnB (EC 4.2.1.3). Tn5::mob insertions occurred additionally in the vicinity of heat shock protein-encoding genes. The predicted function of the LpdA homologue in T. mimigardefordensis is cleavage of the disulfide bond of DTDP to form two molecules of 3MP. Cdo catalyzes the conversion of the sulfhydryl group of 3MP, yielding the corresponding sulfinic acid, 3SP. SucCD exhibits thiokinase activity, ligating coenzyme A (CoA) with 3SP to form 3SP-CoA. Afterwards, an elimination of sulfite via a putative desulfinase is expected. acnB encodes a putative 2-methylisocitrate dehydratase. Therefore, a new pathway is proposed for the catabolism of DTDP via 3MP, 3SP, and 3SP-CoA toward propionyl-CoA, which is then further catabolized via the 2-methylcitric acid cycle in T. mimigardefordensis.

* Corresponding author. Mailing address: Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, 48149 Münster, Germany. Phone: 49-251-8339821. Fax: 49-251-8338388. E-mail: steinbu{at}uni-muenster.de

{triangledown} Published ahead of print on 2 May 2008.

Applied and Environmental Microbiology, July 2008, p. 4028-4035, Vol. 74, No. 13
0099-2240/08/$08.00+0     doi:10.1128/AEM.00422-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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