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Identification of amino acid substitutions in the lipopeptide surfactin using 2D NMR spectroscopy.

Abstract：

:It is generally accepted that surfactin, being produced by various Bacillus subtilis strains, is a cyclic lipopeptide built from the heptapeptide L-Glu-L-Leu-D-Leu-L-Val-L-Asp-D-Leu-L-Leu and a beta-hydroxy fatty acid with variable chain length of 13 - 15 carbon atoms. We investigated surfactin from Bacillus subtilis ATCC 21332 and OKB 105, dissolved in pyridine and methanol, with two-dimensional H NMR spectroscopy. In the NH-fingerprint region, 21 well resolved cross peaks are observed instead of the expected seven cross peaks for the given heptapeptide. We were able to assign all proton signals to 21 amino acids, to identify three heptapeptides, and thus to prove the existence of structural analogues of surfactin. In the major fraction A, the peptide sequence is as given above. In fractions B and C, the C-terminal leucine is replaced by valine and isoleucine, respectively.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Baumgart F,Kluge B,Ullrich C,Vater J,Ziessow D

doi

10.1016/0006-291x(91)90637-m

subject

Has Abstract

pub_date

1991-06-28 00:00:00

pages

998-1005

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)90637-M

journal_volume

177

pub_type

杂志文章

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