ADP-Ribosylargininyl reaction of cholix toxin is mediated through diffusible intermediates

BMC Biochemistry

Table 1 Cholix toxin catalytic fragment variants contain arginine (R) to lysine (K) replacement mutations

R to K mutants	R to K replacement mutations on the wild type CTc	^ǂ Auto-ADP-ribosylation activity	^¶ NAD ⁺ glycohydrolase activity
M1	R506K,R566K	170	150.7 ± 1
M2	R426K,R473K,R506K,R566K,R629K	205	173 ± 3.4
M4	R426K,R473K,R506K,R519K,R522K,R566K,R629K	250	197.8 ± 4.6
M4392	R426K,R473K,R506K,R519K,R522K,R540K,R566K,R629K	113	105.4 ± 1
M4421	R426K,R473K,R506K,R519K,R522K,R543K,R566K,R629K	100	79.4 ± 5.9
M4781	R426K,R473K,R479K,R506K,R519K,R522K,R566K,R629K	130	126.6 ± 2
M5-2	R426K,R473K,R506K,R519K,R522K,R540K,R543K,R566K,R629K	100	7.8 ± 1.7
M5-4	R426K,R451K,R473K,R506K,R519K,R522K,R540K,R543K,R566K,R629K	155	8.2 ± 0.8
M6	R426K,R451K,R473K,R506K,R519K,R522K,R535K,R540K,R543K,R566K,R629K	90	9.6 ± 1.8
M6781	R426K,R451K,R473K,R479K,R506K,R519K,R522K,R535K,R540K,R543K,R566K,R629K	0	50 ± 1.5
M7	R426K,R451K,R473K,R506K,R519K,R522K,R525K,R535K,R540K,R543K,R566K,R629K	70	1 ± 3
M8	R426K,R451K,R473K,R479K,R506K,R519K,R522K,R525K,R535K,R540K,R543K,R566K,R629K	0	52.1 ± 1.7
WT	*-	215	206.3 ± 8.6

^ǂ Data show the mean fluorescence of intensity of biotin signals on the auto-ADP-ribosylated enzyme band detected by IRDye800-SA.
^¶Data show the specific activity of each enzyme as described in Methods.
*Wild type cholix toxin catalytic fragment (WT) contains R426, R451, R473, R479, R506, R519, R522, R525, R530, R535, R540, R543, R566, R629.

ISSN: 1471-2091