| pubmed-article:7559521 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C1449830 | lld:lifeskim |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C2248654 | lld:lifeskim |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:7559521 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:7559521 | pubmed:issue | 40 | lld:pubmed |
| pubmed-article:7559521 | pubmed:dateCreated | 1995-11-14 | lld:pubmed |
| pubmed-article:7559521 | pubmed:abstractText | The CobU protein of Salmonella typhimurium was overexpressed and purified to approximately 94% homogeneity. N-terminal sequencing of purified CobU confirmed the first 22 amino acids. In vitro assays showed that CobU has kinase and guanylyltransferase activities which catalyze the synthesis of adenosyl-cobinamide-GDP from adenosyl-cobinamide, via an adenosyl-cobinamide-phosphate intermediate. We present evidence that the transfer of the guanylyl moiety of GTP to adenosyl-cobinamide-phosphate proceeds via an phosphoramidate-linked, enzyme-guanylyl intermediate. In the presence of oxygen, kinase and guanylyltransferase activities of CobU were lost. Treatment of inactive CobU with dithiothreitol restored approximately 20% of the kinase and guanylyltransferase activities, indicating the involvement of sulfhydryl groups in enzyme activity. The sulfhydryl modifying agents 5,5'-dithiobis(2-nitrobenzoic acid) and N-ethylmaleimide abolished both CobU activities. Native CobU protein was a dimer (approximately 40 kDa) that functioned optimally at pH 8.8-9.0 and 37 degrees C. Substrates and kinetic parameters for both activities were determined. The preferred corrinoid substrate for this enzyme was adenosyl-cobinamide. In vitro experiments are consistent with previous genetic studies which had suggested that adenosyl-cobinamide was the preferred substrate of CobU, and that CobU functioned more efficiently in the absence of oxygen. | lld:pubmed |
| pubmed-article:7559521 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7559521 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7559521 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7559521 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7559521 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7559521 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7559521 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7559521 | pubmed:author | pubmed-author:Escalante-Sem... | lld:pubmed |
| pubmed-article:7559521 | pubmed:author | pubmed-author:O'TooleG AGA | lld:pubmed |
| pubmed-article:7559521 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7559521 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:7559521 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7559521 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7559521 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7559521 | pubmed:pagination | 23560-9 | lld:pubmed |
| pubmed-article:7559521 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7559521 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7559521 | pubmed:articleTitle | Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate. | lld:pubmed |
| pubmed-article:7559521 | pubmed:affiliation | Department of Bacteriology, University of Wisconsin, Madison 53706, USA. | lld:pubmed |
| pubmed-article:7559521 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7559521 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7559521 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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