| pubmed-article:10878136 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10878136 | lifeskim:mentions | umls-concept:C0317472 | lld:lifeskim |
| pubmed-article:10878136 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10878136 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:10878136 | lifeskim:mentions | umls-concept:C1150393 | lld:lifeskim |
| pubmed-article:10878136 | lifeskim:mentions | umls-concept:C0752078 | lld:lifeskim |
| pubmed-article:10878136 | pubmed:dateCreated | 2000-8-30 | lld:pubmed |
| pubmed-article:10878136 | pubmed:abstractText | Vancomycin resistance in Enterococcus gallinarum results from the production of UDP-MurNAc-pentapeptide[D-Ser]. VanT, a membrane-bound serine racemase, is one of three proteins essential for this resistance. To investigate the selectivity of racemization of L-Ser or L-Ala by VanT, a strain of Escherichia coli TKL-10 that requires D-Ala for growth at 42 degrees C was used as host for transformation experiments using plasmids containing the full-length vanT from Ent. gallinarum or the alanine racemase gene (alr) of Bacillus stearothermophilus: both plasmids were able to complement E. coli TKL-10 at 42 degrees C. No alanine or serine racemase activities were detected in the host strain E. coli TKL-10 grown at 30, 34 or 37 degrees C. Serine and alanine racemase activities were found almost exclusively (96%) in the membrane fraction of E. coli TKL-10/pCA4(vanT): the alanine racemase activity of VanT was 14% of the serine racemase activity in both E. coli TKL-10/pCA4(vanT) and E. coli XL-1 Blue/pCA4(vanT). Alanine racemase activity was present mainly (95%) in the cytoplasmic fraction of E. coli TKL-10/pJW40(alr), with a trace (1.6%) of serine racemase activity. Additionally, DNA encoding the soluble domain of VanT was cloned and expressed in E. coli M15 as a His-tagged polypeptide and purified: this polypeptide also exhibited both serine and alanine racemase activities; the latter was approximately 18% of the serine racemase activity, similar to that of the full-length, membrane-bound enzyme. N-terminal sequencing of the purified His-tagged polypeptide revealed a single amino acid sequence, indicating that the formation of heterodimers between subunits of His-tagged C-VanT and endogenous alanine racemases from E. coli was unlikely. The authors conclude that the membrane-bound serine racemase VanT also has alanine racemase activity but is able to racemize serine more efficiently than alanine, and that the cytoplasmic domain is responsible for the racemase activity. | lld:pubmed |
| pubmed-article:10878136 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10878136 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10878136 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10878136 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10878136 | pubmed:issn | 1350-0872 | lld:pubmed |
| pubmed-article:10878136 | pubmed:author | pubmed-author:ReynoldsP EPE | lld:pubmed |
| pubmed-article:10878136 | pubmed:author | pubmed-author:AriasC ACA | lld:pubmed |
| pubmed-article:10878136 | pubmed:author | pubmed-author:BlackburnJ... | lld:pubmed |
| pubmed-article:10878136 | pubmed:author | pubmed-author:WeisnerJJ | lld:pubmed |
| pubmed-article:10878136 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10878136 | pubmed:volume | 146 ( Pt 7) | lld:pubmed |
| pubmed-article:10878136 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10878136 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10878136 | pubmed:pagination | 1727-34 | lld:pubmed |
| pubmed-article:10878136 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10878136 | pubmed:meshHeading | pubmed-meshheading:10878136... | lld:pubmed |
| pubmed-article:10878136 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10878136 | pubmed:articleTitle | Serine and alanine racemase activities of VanT: a protein necessary for vancomycin resistance in Enterococcus gallinarum BM4174. | lld:pubmed |
| pubmed-article:10878136 | pubmed:affiliation | Department of Biochemistry, University of Cambridge, Tennis Court Road, The Downing Site, Cambridge CB2 1QW, UK. caa22@cable.net.co | lld:pubmed |
| pubmed-article:10878136 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10878136 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10878136 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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