Boguslaw Kluge

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The lipopeptide antibiotic surfactin is a potent extracellular biosurfactant produced by various Bacillus subtilis strains. Biosynthesis of surfactin was studied in a cell-free system prepared from B. subtilis ATCC 21332 and OKB 105, which is a transformant producing surfactin in high yield [Nakano, M. M., Marahiel, M. A., & Zuber, P. (1988) J. Bacteriol.(More)
By gel filtration of a crude extract of Bacillus subtilis ATCC 21332 and OKB 105, the multienzyme system that forms the lipoheptapeptide surfactin was separated into three enzyme fractions, E1, E2, and E3. E1, which appeared near the exclusion limit of the column, activates all amino acid components of surfactin as aminoacyladenylates and thioesters(More)
The biosynthesis of the lipopeptide antibiotic surfactin was studied in whole cells of Bacillus subtilis ATCC 21332 which incorporate 14C-labeled precursor amino acids directly into the product. [14C]Acetate appeared in the fatty acid portion of surfactin and was also partially converted into leucine. An enzyme was isolated and partially purified from a(More)
The biosynthesis of the decapeptide antibiotic gramicidin S in Bacillus brevis ATCC 9999 is catalyzed by a multienzyme system consisting of two multifunctional proteins, gramicidin S synthetase 1 and 2, encoded by the grsA and grsB genes, respectively. Gramicidin S synthetase 1 (phenylalanine racemase, EC 5.1.1.11, GS1) racemizes phenylalanine in the(More)
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(More)
The reactive serine of the TGGHSL thioester binding motif of the first amino acid-activating domain of surfactin synthetase was replaced by alanine using site-directed mutagenesis. The multienzyme from cells of the resulting mutant lost its ability for thioester formation with L-Glu and was therefore inactive in surfactin production. The thiolation(More)
R.MwoI is a Type II restriction endonucleases enzyme (REase), which specifically recognizes a palindromic interrupted DNA sequence 5'-GCNNNNNNNGC-3' (where N indicates any nucleotide), and hydrolyzes the phosphodiester bond in the DNA between the 7th and 8th base in both strands. R.MwoI exhibits remote sequence similarity to R.BglI, a REase with known(More)
Recent studies demonstrate that the peptides in the serum of cancer patients that are generated (ex vivo) as a result of tumor protease activity can be used for the detection and classification of cancer. In this paper, we propose the first formal approach to modeling exopeptidase activity from liquid chromatography-mass spectrometry (LC-MS) samples. We(More)
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