| pubmed-article:6803772 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6803772 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:6803772 | lifeskim:mentions | umls-concept:C0033617 | lld:lifeskim |
| pubmed-article:6803772 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6803772 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:6803772 | lifeskim:mentions | umls-concept:C0066310 | lld:lifeskim |
| pubmed-article:6803772 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6803772 | pubmed:dateCreated | 1982-6-24 | lld:pubmed |
| pubmed-article:6803772 | pubmed:abstractText | A methyltransferase that methylates one of the proteins involved in chemotactic adaptation to sensory stimuli in Bacillus subtilis was purified to homogeneity. The enzyme utilizes S-adenosylmethionine as donor for a methyl group that is transferred to a glutamate residue in a 69 000-mol.wt. membrane protein and also to a protein of 19 000 mol.wt. The molecular weights of the denatured enzyme by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and of the native enzyme by gel-filtration chromatography both show the protein to be a 44 000-mol.wt. monomer. Isoelectric focusing of the purified methyltransferase showed the protein to be a single species with isoelectric point pI 5.4. On the basis of a molecular weight of 44 000, the molar absorption coefficient at 262 nm of the enzyme is 10.9 x 10(4) M-1 . cm-1. The Km of the enzyme for S-adenosylmethionine is about 2 microM. The Ki for S-adenosylhomocysteine is about 0.2 microM. Ca2+ is a competitive inhibitor of methylation, with a Ki of 0.065 microM. The enzyme methylates membranes from the wild-type more efficiently than membranes isolated from a mutant strain defective in chemotaxis. The enzyme is unable to methylate Escherichia coli membranes. | lld:pubmed |
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| pubmed-article:6803772 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6803772 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6803772 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6803772 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:6803772 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6803772 | pubmed:author | pubmed-author:OrdalG WGW | lld:pubmed |
| pubmed-article:6803772 | pubmed:author | pubmed-author:UllahA HAH | lld:pubmed |
| pubmed-article:6803772 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6803772 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6803772 | pubmed:volume | 199 | lld:pubmed |
| pubmed-article:6803772 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6803772 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6803772 | pubmed:pagination | 795-805 | lld:pubmed |
| pubmed-article:6803772 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:6803772 | pubmed:meshHeading | pubmed-meshheading:6803772-... | lld:pubmed |
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| pubmed-article:6803772 | pubmed:meshHeading | pubmed-meshheading:6803772-... | lld:pubmed |
| pubmed-article:6803772 | pubmed:meshHeading | pubmed-meshheading:6803772-... | lld:pubmed |
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| pubmed-article:6803772 | pubmed:meshHeading | pubmed-meshheading:6803772-... | lld:pubmed |
| pubmed-article:6803772 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:6803772 | pubmed:articleTitle | Purification and characterization of methyl-accepting chemotaxis protein methyltransferase I in Bacillus subtilis. | lld:pubmed |
| pubmed-article:6803772 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6803772 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6803772 | lld:pubmed |
