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J. Biol. Chem., Vol. 266, Issue 34, 23135-23141, Dec, 1991
W Schlumbohm, T Stein, C Ullrich, J Vater, M Krause, MA Marahiel, V Kruft and B Wittmann-Liebold
The condensing peptide forming multienzyme of gramicidin S synthetase
(gramicidin S synthetase 2) was specifically labeled at its putative
thiotemplate sites for L-valine and L-leucine by covalent incorporation of
the 14C-labeled substrate amino acids. The thioester complexes of the
multienzyme were digested with CNBr, Staphylococcus aureus V8 protease, and
pepsin. Reaction center peptides containing the [14C]valine and
[14C]leucine labels were isolated in pure form. They show a high degree of
sequence similarity and contain the same consensus sequence LGGH/DXL. The
labels were eliminated in the first Edman degradation step. A
dehydroalanine was identified which can originate from either a cysteine or
a serine. The comparison of the chemical results with the deduced amino
acid sequence of the grsB gene encoding the gramicidin S synthetase 2
revealed that 4 such motifs are located within the gene structure, each of
them being localized in the 3'-terminal region of one of 4 gene segments
grsB1-B4. They have a size of approximately 2 kilobases and presumably code
for the 4 amino acid activating domains of the synthetase. Surprisingly a
serine was found at each putative substrate amino acid-binding position
instead of a cysteine as postulated by the thiotemplate mechanism.
Therefore the data suggest that active serine residues are involved in
nonribosomal peptide syntheses of microbial peptides.
An active serine is involved in covalent substrate amino acid binding at each reaction center of gramicidin S synthetase
Institute of Biochemistry and Molecular Biology, Technical University of Berlin, Federal Republic of Germany.
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