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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1990-8-7
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pubmed:abstractText |
DD-Carboxypeptidase (DD-CPase) activity of Enterococcus hirae (Streptococcus faecium) ATCC 9790 was extracted from intact bacteria and from the insoluble residue (crude cell wall fraction) of mechanically disrupted bacteria by a brief treatment at pH 10.0 (10 mM glycine-NaOH) at 0 degrees C or by extraction with any of several detergents. Extractions with high salt concentrations failed to remove DD-CPase activity from the crude wall fraction. In contrast to N-acetylmuramoylhydrolase (both muramidase 2 and muramidase 1) activities, DD-CPase activity failed to bind to insoluble cell walls or peptidoglycan matrices. Thus, whereas muramidase 1 and muramidase 2 activities can be considered to be cell wall proteins, the bulk of the data are consistent with the interpretation that the DD-CPase of this species is a membrane protein that is sometimes found in the cell wall fraction, presumably because of hydrophobic interactions with other proteins and cell wall polymers. The binding of [14C]penicillin to penicillin-binding protein 6 (43 kilodaltons) was proportional to DD-CPase activity. Kinetic parameters were also consistent with the presence of only one DD-CPase (penicillin-binding protein 6) in E. hirae.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2361945-1012018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2361945-110765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2361945-1391,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2361945-2753858,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
172
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3718-24
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2361945-Cell Membrane,
pubmed-meshheading:2361945-Cell Wall,
pubmed-meshheading:2361945-Hydrogen-Ion Concentration,
pubmed-meshheading:2361945-Kinetics,
pubmed-meshheading:2361945-Molecular Weight,
pubmed-meshheading:2361945-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:2361945-Penicillin G,
pubmed-meshheading:2361945-Protein Binding,
pubmed-meshheading:2361945-Protoplasts,
pubmed-meshheading:2361945-Streptococcus,
pubmed-meshheading:2361945-Ultracentrifugation
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pubmed:year |
1990
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pubmed:articleTitle |
Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali.
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pubmed:affiliation |
Department of Microbiology and Immunology, School of Medicine, Temple University, Philadelphia, Pennsylvania 19140.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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