Structural characterization of lichenysin A components by fast atom bombardment tandem mass spectrometry
Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid
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Yn: Biochimica et Biophysica Acta (BBA), Cyfrol 1438, Rhif 2, 18.05.1999, t. 273-80.
Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid
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T1 - Structural characterization of lichenysin A components by fast atom bombardment tandem mass spectrometry
AU - Yakimov, M M
AU - Abraham, W R
AU - Meyer, Holger
AU - Laura Giuliano, null
AU - Golyshin, P N
PY - 1999/5/18
Y1 - 1999/5/18
N2 - 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.
AB - 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.
KW - Bacillus/chemistry
KW - Lipoproteins/chemistry
KW - Molecular Structure
KW - Peptides, Cyclic/chemistry
KW - Spectrometry, Mass, Fast Atom Bombardment
M3 - Article
C2 - 10320810
VL - 1438
SP - 273
EP - 280
JO - Biochimica et Biophysica Acta (BBA)
JF - Biochimica et Biophysica Acta (BBA)
SN - 0006-3002
IS - 2
ER -