Linked Life Data

18297793

Source:http://linkedlifedata.com/resource/pubmed/id/18297793

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-2-26
pubmed:abstractText
A bacterium capable to grow on sulfanilic acid as sole carbon, nitrogen and sulfur source has been isolated. A unique feature of this strain is that it contains the full set of enzymes necessary for the biodegradation of sulfanilic acid. Taxonomical analysis identified our isolate as Sphingomonas subaretica SA1 sp. The biodegradation pathway of sulfanilic acid was investigated at the molecular level. Screening the substrate specificity of the strain disclosed its capacity to degrade six analogous aromatic compounds including p-aminobenzoic acid. Moreover, the strain was successfully used for removal of oil contaminations. S. subarctica SA1 seemed to use distinct enzyme cascades for decomposition of these molecules, since alternative enzymes were induced in cells grown on various substrates. However, the protein patterns appearing upon induction by sulfanilic acid and sulfocatechol were very similar to each other indicating common pathways for the degradation of these substrates. Cells grown on sulfanilic acid could convert p-aminobenzoic acid to some extent and vice versa. Two types of ring cleaving dioxygenases were detected in the cells grown on various substrates: one preferred protocatechol, while the other had higher activity with sulfocatechol. This latter enzyme, named as sulfocatechol dioxygenase was partially purified and characterized.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0236-5383
pubmed:author
pubmed:issnType
Print
pubmed:volume
58 Suppl
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-49
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Overlaps between the various biodegradation pathways in Sphingomonas subarctica SA1.
pubmed:affiliation
Department of Biotechnology, University of Szeged, Szeged, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't