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Studies on the biosynthesis of surfactin, a lipopeptide antibiotic from Bacillus subtilis ATCC 21332
Author(s) -
Kluge Britta,
Vater Joachim,
Salnikow Johann,
Eckart Klaus
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80712-9
Subject(s) - surfactin , bacillus subtilis , lipopeptide , biosynthesis , biochemistry , amino acid , peptide , chemistry , enzyme , leucine , substrate (aquarium) , bacteria , biology , ecology , genetics
The biosynthesis of the lipopeptide antibiotic surfactin was studied in whole cells of Bacillus subtilis ATCC 21332 which incorporate 14 C‐labeled precursor amino acids directly into the product. [ 14 C]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 cell‐free extract of the bacillus which catalyzes ATP‐P i ‐exchange reactions which are mediated by the amino acid components of surfactin. This activation pattern is consistent with a peptide synthesizing multienzyme which activates its substrate amino acids simultaneously as reactive aminoacyl phosphates.