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. 2011 Sep 29;6(9):e25312. doi: 10.1371/journal.pone.0025312

Table 4. Residues involved in ATP inhibition for human wild-type and nucleotide-binding mutant c-NADP-ME variants.

c-NADP-ME Residue aATP inhibition (%)
314 346 347 362 bNAD+ bNADP+
WT E S K K 87.3 99.4
E314A A S K K 47.3 96.6
S346K E K K K 83.8 96.8
E314A/S346K A K K K 33.2 99.3
K347Y E S Y K 94.2 96.6
K362Q E S K Q 95.4 99.8
K362H E S K H 88.0 89.3
S346K/K347Y E K Y K 75.2 86.7
S346K/K362Q E K K Q 86.5 91.8
K347Y/K362Q E S Y Q 99.2 91.6
S346K/K347Y/K362Q E K Y Q 71.4 81.3
E314A/S346K/K347Y/K362Q A K Y Q 64.5 64.7
S346K/K347Y/K362H E K Y H 82.9 78.8
E314A/S346K/K347Y/K362H A K Y H 76.2 75.0
S346I/K347D/K362H E I D H 88.5 83.1
E314A/S346I/K347D/K362H A I D H 98.6 90.6
a

Residual enzyme activity by inhibition at 3 mM ATP.

b

using NAD+ or NADP+ as the cofactor.