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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2009-9-16
pubmed:abstractText
Eubacteria can import and simultaneously phosphorylate a range of different carbohydrates by means of sugar specific phosphoenolpyruvate (PEP) dependent sugar phosphotransferase systems (PTSs). Here, we report the biochemical characterization of the gluconate specific PTS component EIIA(gnt) from Enterococcus faecalis and its unexpectedly strong complex with EIIB(gnt). We analyze the activity of the complex regarding phosphoryl transfer using kinetic measurements and demonstrate by mutagenesis that His-9 of EIIA(gnt) is essential for this process and represents most likely the phosphoryl group carrier of EIIA(gnt). With a combination of isothermal titration calorimetry (ITC), analytical ultracentrifugation (AUC), native gel electrophoresis and chemical crosslinking experiments we show that EIIA(gnt) and EIIB(gnt) form a strong 2:2 heterotetrameric complex, which seems to be destabilized upon phosphorylation of EIIB(gnt).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
30
pubmed:volume
388
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
630-6
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Activity of the Enterococcus faecalis EIIA(gnt) PTS component and its strong interaction with EIIB(gnt).
pubmed:affiliation
AG Physiology of Microorganisms, Ruhr-Universität Bochum, 44780 Bochum, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't