Linked Life Data

10320810

Source:http://linkedlifedata.com/resource/pubmed/id/10320810

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-6-17
pubmed:abstractText
The structural characterization of the cyclic lipoheptapeptide surfactant lichenysin A components, produced by Bacillus licheniformis strains via the non-ribosomal pathway on a corresponding peptide synthetase, was carried out using a tandem mass spectrometry (MS/MS) under fast atom bombardment (FAB) conditions. Based on the analysis of the collision-induced fragment-ion spectrum of the single charged molecular ions of both native and partially hydrolyzed forms of lipopeptide, a new general structure of lichenysin A components was elucidated. It varies from previously proposed structure by having in the peptide portion of lipopeptide the L-Gln-1 and L-Asp-5 residues instead of L-Glu-1 and L-Asn-5. The verified chemical structure of lichenysin A was found to be reflected in the structural organization of the corresponding lichenysin A synthetase, LchA, described recently.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
1438
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Structural characterization of lichenysin A components by fast atom bombardment tandem mass spectrometry.
pubmed:affiliation
Department of Microbiology, GBF National Research Center for Biotechnology, Mascheroder Weg 1, 38124, Braunschweig, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't