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. 2014 May 7;9(5):e96627. doi: 10.1371/journal.pone.0096627

Table 3. Mutational effects on the catalytic activity (k cat/K m ratio) and thermal stability (ΔT m) of Sfβgly proteins.

Mutation position kcat/K m ratio (mutant/wt) ΔTm (K)
NPβglc NPβgal NPβfuc
49 0.5 0.06 0.7 −7.2
54 0.02 0.005 0.02 −0.2
57 0.77 0.12 0.8 −1.0
62 0.09 0.03 0.18 −5.5
98 - - - −2.1
112 1.5 0.19 0.38 −0.3
143 0.0004 0.0003 0.0005 −7.2
188 0.0002 0.0011 0.0012 3.2
195 0.11 0.01 0.03 0.1
196 0.06 0.01 0.06 0.0
203 0.06 0.04 0.21 0.8
223 0.30 0.05 0.075 6.0
278 0.005 0.02 0.02 5.8
309 0.15 0.02 0.02 −7.1
398 - - - nd
445 1.1 1.5 0.27 −1.9
452 - - - −2.8
460 0.0012 0.0037 0.0044 −12.2

Only mutational effects higher than a 4-fold change in the k cat/K m ratio (0.25>k cat/K m ratio >4) were considered significant for the enzymatic activity. Mutational effects on the thermal stability were considered relevant only for ΔTm>2.5 K. –, no activity; nd, not determined; wt, wild-type.