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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1979-8-16
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pubmed:abstractText |
The initial membrane reaction in the biosynthesis of peptidoglycan is catalyzed by phospho-N-acetylmuramyl (MurN Ac)-pentapeptide translocase (UDP-MurNAc-Ala-gamma DGlu-Lys-DAla-DAla undecaprenyl phosphate phospho-MurNAc-pentapeptide transferase). In addition to the transfer reaction, the enzyme catalyzes the exchange of [3H]uridine monophosphate with the uridine monophosphate moiety of UDP-MurN Ac-pentapeptide. Two distinct discontinuities are observed in the slopes of the Arrhenius plots of the exchange and transfer activities at 22 and 30 degrees C for the enzyme from Staphylococcus aureus Copenhagen. Anisotropy measurements of perylene fluorescence and electron spin resonance measurements of N-oxyl-4',4'-dimethyloxazolidine derivatives of 12- and 16-ketostearic acid intercalated into membranes from this organism define the lower (T1 = 16--22 degrees C) and upper (Th = 30 degrees C) boundaries of a phase transition. These values correlate with the discontinuities observed for the activity measurements. Thus, it is proposed that the physical state of the lipid micro-environment of phospho-MurNAc-penetapeptide translocase has a significant effect on the catalytic activity of this enzyme.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
|
pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
552
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
418-27
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1979
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pubmed:articleTitle |
Initial membrane reaction in peptidoglycan synthesis. Interaction of lipid with phospho-N-acetylmuramyl-pentapeptide translocase.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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