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. 2017 Aug 24;7:9330. doi: 10.1038/s41598-017-09575-6

Table 2.

Acylation status of different CyaA mutants.

Proteina K860 K983
Palmitoleyl (%)c Palmitoyl (%)c Palmitoleyl (%)c Palmitoyl (%)c
proCyaAb 0.2 0 3.6 0.8
CyaA 44.3 45.9 55.9 22.1
CyaA-Y940F 38.1 57.8 41.6 20.8
CyaA-Y940A 39.3 55.8 56.8 22.4
CyaA-Y940P 42.9 50.9 55.9 19.8

aAll CyaA proteins were produced in the E. coli strain XL1-Blue and purified close to homogeneity.

bThe proCyaA variant was expressed in the absence of the CyaC acyltransferase.

cPercentage distribution of fatty acid modification of the ε-amino groups of the K860 and K983 residues by palmitoleyl (cisΔ9 C16:1) and palmitoyl (C16:0) chains. Average values are derived from determinations performed with two different toxin preparations. The remaining Lys860 and Lys983 residues to 100% are non-acylated.