Document Detail


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.
MedLine Citation:
PMID:  18456849     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The hitherto unstudied microbial degradation of the organic disulfide 3,3'-dithiodipropionic acid (DTDP) was investigated with the recently described bacterium Tetrathiobacter mimigardefordensis strain DPN7(T) (DSM 17166(T); LMG 22922(T)), 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.
Authors:
Jan Hendrik Wübbeler; Nadine Bruland; Kornelia Kretschmer; Alexander Steinbüchel
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Publication Detail:
Type:  Journal Article     Date:  2008-05-02
Journal Detail:
Title:  Applied and environmental microbiology     Volume:  74     ISSN:  1098-5336     ISO Abbreviation:  Appl. Environ. Microbiol.     Publication Date:  2008 Jul 
Date Detail:
Created Date:  2008-06-27     Completed Date:  2008-07-29     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  7605801     Medline TA:  Appl Environ Microbiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4028-35     Citation Subset:  IM    
Affiliation:
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, 48149 Münster, Germany.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/EU423868;  EU423869;  EU423870;  EU423871
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MeSH Terms
Descriptor/Qualifier:
3-Mercaptopropionic Acid / metabolism
Acyl Coenzyme A / metabolism*
Aerobiosis
Alcaligenaceae / enzymology,  genetics,  growth & development,  metabolism*
Molecular Sequence Data
Organic Chemicals / metabolism*
Propionates / chemistry,  metabolism*
Sequence Analysis, DNA
Sulfur Compounds / chemistry,  metabolism*
Chemical
Reg. No./Substance:
0/Acyl Coenzyme A; 0/Organic Chemicals; 0/Propionates; 0/Sulfur Compounds; 107-96-0/3-Mercaptopropionic Acid; 317-66-8/propionyl-coenzyme A; 52329-65-4/3-sulfinopropionic acid; 79-09-4/propionic acid
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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