In:
FEBS Letters, Wiley, Vol. 231, No. 1 ( 1988-04-11), p. 107-110
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(88)80712-9
Language:
English
Publisher:
Wiley
Publication Date:
1988
detail.hit.zdb_id:
1460391-3
SSG:
12
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