Biosynthesis of bacillomycin D by Bacillus subtilis Evidence for amino acid‐activating enzymes by the use of affinity chromatography

FEBS Letters

Besson, Françoise¹  Michel, Georges¹ 

[1] Laboratoire de Biochimie Microbienne (CNRS UMR 24), Université Claude-Bernard Lyon I, 43 Boulevard du 11 novembre 1918, F-69622 Villeurbanne Cedex, France

关键词: Bacillomycin D;    Antibiotic lipopeptide biosynthesis;    Amino acid activation;    Affinity chromatography;    Bacillus subtilis;    BSA;    bovine serum albumin;    CP preparation;    crude protein preparation;    DTT;    dithiothreitol;    EDTA;    ethylenediaminetetraacetic acid;    HPLC;    high-performance liquid chromatography;    Pi;    inorganic phosphate;    PPi;    inorganic pyrophosphate;    SDS;    sodium dodecyl sulfate;    TCA;    trichloroacetic acid;    TLC;    thin layer chromatography;    Tris;    tris(hydroxymethyl)aminomethane;   

DOI  :  10.1016/0014-5793(92)81040-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bacillomycin D is an antifungal lipopeptide produced by B. subtilis. The formation of the peptidyl bonds of bacillomycin D occurs non-ribosomally, as demonstrated by the use of chloramphenicol, an inhibitor of protein biosynthesis. Amino acid-activating enzymes were found in B. subtilis cell lysates purified by affinity chromatography on a gel containing l-Pro, an amino acid of bacillomycin D. Presence of ATP during this purification increases the binding of enzymatic proteins and their activity. An enzyme, with an apparent molecular weight of 230 kDa, catalyzed ATP-PPi exchange reactions, which were mediated by specific amino acids, corresponding to a partial sequence of bacillomycin D.

【 授权许可】

Unknown