PMID:7801126

Citation	Stanley, P, Packman, LC, Koronakis, V and Hughes, C (1994) Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin. Science 266:1992-6
Abstract	Hemolysin of Escherichia coli is activated by fatty acylation of the protoxin, directed by the putative acyl transferase HlyC and by acyl carrier protein (ACP). Mass spectrometry and Edman degradation of proteolytic products from mature toxin activated in vitro with tritium-labeled acylACP revealed two fatty-acylated internal lysine residues, lysine 564 and lysine 690. Resistance of the acylation to chemical treatments suggested that fatty acid was amide linked. Substitution of the two lysines confirmed that they were the only sites of acylation and showed that although each was acylated in the absence of the other, both sites were required for in vivo toxin activity.
Links	PubMed
Keywords	Acyl Carrier Protein/metabolism; Acylation; Acyltransferases/metabolism; Amino Acid Sequence; Animals; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Bacterial Proteins/toxicity; Bacterial Toxins/chemistry; Bacterial Toxins/metabolism; Bacterial Toxins/toxicity; Escherichia coli; Escherichia coli Proteins; Hemolysin Proteins/chemistry; Hemolysin Proteins/metabolism; Hemolysin Proteins/toxicity; Hemolysis; Horses; Lysine/metabolism; Mass Spectrometry; Molecular Sequence Data; Protein Precursors/metabolism; Sequence Alignment
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