The amino acid sequence in bacitracin A

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Abstract
Bacitracin A was subjected to partial hydrolysis with acid and the resulting peptides were fractionated by ionophoresis in a 4-compartment cell by paper chromatography, and by ionophoresis on paper. Similar experiments were carried out with commercial bacitracin, also with commercial bacitracin that was inactivated with acid and subsequently converted into an S-methyl derivative or desulfurized. Most of the peptides obtained from both bacitracin A and commercial bacitracin were consistent with the presence of the following sequence, in which a branch arises at the lysine residue:[image] Several peptides indicate that the histidine and phenylalanine residues in bacitracin A are linked together to form a ring. Others suggested that the phenylalanine residue may also interact with the isoleucine residue which is next to the potential cysteine. Peptides from commercial bacitracin which contain "valine" suggest that the sequence Lys. Orn. Val. Phe. occurs in bacitracin B.