| pubmed-article:2361945 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0085495 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0317474 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0002055 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0185115 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C2265036 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0598079 | lld:lifeskim |
| pubmed-article:2361945 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:2361945 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2361945 | pubmed:dateCreated | 1990-8-7 | lld:pubmed |
| pubmed-article:2361945 | 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. | lld:pubmed |
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| pubmed-article:2361945 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2361945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2361945 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2361945 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2361945 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2361945 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2361945 | pubmed:author | pubmed-author:ShockmanG DGD | lld:pubmed |
| pubmed-article:2361945 | pubmed:author | pubmed-author:Daneo-MooreLL | lld:pubmed |
| pubmed-article:2361945 | pubmed:author | pubmed-author:KariyamaRR | lld:pubmed |
| pubmed-article:2361945 | pubmed:author | pubmed-author:MassiddaOO | lld:pubmed |
| pubmed-article:2361945 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2361945 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:2361945 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2361945 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2361945 | pubmed:pagination | 3718-24 | lld:pubmed |
| pubmed-article:2361945 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2361945 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2361945 | pubmed:articleTitle | Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali. | lld:pubmed |
| pubmed-article:2361945 | pubmed:affiliation | Department of Microbiology and Immunology, School of Medicine, Temple University, Philadelphia, Pennsylvania 19140. | lld:pubmed |
| pubmed-article:2361945 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2361945 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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