| pubmed-article:7826328 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C0317761 | lld:lifeskim |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C0142281 | lld:lifeskim |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7826328 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:7826328 | pubmed:dateCreated | 1995-2-16 | lld:pubmed |
| pubmed-article:7826328 | pubmed:abstractText | The extracellular siderophore from Mycobacterium smegmatis, exochelin MS, was isolated from iron-deficiently grown cultures and purified to > 98% by a combination of ion-exchange chromatography and h.p.l.c. The material is unextractable into organic solvents, is basic (pI = 9.3-9.5), has a lambda max at 420 nm and a probable Ks for Fe3+ of between 10(25) and 10(30). Its structure has been determined by examination of desferri- and ferri-exochelin and its gallium complex. The methods used were electrospray-m.s. and one- and two-dimensional (NOESY, DQF-COSY and TOCSY) 1H n.m.r. The constituent amino acids were examined by chiral g.l.c analysis of N-trifluoroacetyl isopropyl and N-pentafluoropropionyl methyl esters after hydrolysis, and reductive HI hydrolysis, of the siderophore. The exochelin is a formylated pentapeptide: N-(delta-N-formyl,delta N-hydroxy-R-ornithyl) -beta-alaninyl-delta N-hydroxy-R-ornithinyl-R-allo-threoninyl-delta N-hydroxy-S-ornithine. The linkages involving the three ornithine residues are via their delta N(OH) and alpha-CO groups leaving three free alpha-NH2 groups. Although there are two peptide bonds, these involve the three R (D)-amino acids. Thus the molecule has no conventional peptide bond, and this suggests that it will be resistant to peptidase hydrolysis. The co-ordination centre with Fe3+ is hexadenate in an octahedral structure involving the three hydroxamic acid groups. Molecular modelling shows it to have similar features to other ferric trihydroxamate siderophores whose three-dimensional structures have been established. The molecule is shown to have little flexibility around the iron chelation centre, although the terminal (Orn-3) residue, which is not involved in iron binding except at its delta N atom, has more motional freedom. | lld:pubmed |
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| pubmed-article:7826328 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7826328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7826328 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7826328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7826328 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7826328 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7826328 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7826328 | pubmed:author | pubmed-author:RatledgeCC | lld:pubmed |
| pubmed-article:7826328 | pubmed:author | pubmed-author:WilliamsD HDH | lld:pubmed |
| pubmed-article:7826328 | pubmed:author | pubmed-author:EwingD FDF | lld:pubmed |
| pubmed-article:7826328 | pubmed:author | pubmed-author:SharmanG JGJ | lld:pubmed |
| pubmed-article:7826328 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7826328 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7826328 | pubmed:volume | 305 ( Pt 1) | lld:pubmed |
| pubmed-article:7826328 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7826328 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7826328 | pubmed:pagination | 187-96 | lld:pubmed |
| pubmed-article:7826328 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7826328 | pubmed:meshHeading | pubmed-meshheading:7826328-... | lld:pubmed |
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| pubmed-article:7826328 | pubmed:meshHeading | pubmed-meshheading:7826328-... | lld:pubmed |
| pubmed-article:7826328 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7826328 | pubmed:articleTitle | Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis. | lld:pubmed |
| pubmed-article:7826328 | pubmed:affiliation | Department of Chemistry, Cambridge University, U.K. | lld:pubmed |
| pubmed-article:7826328 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7826328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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