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. 2006 Nov 14;400(Pt 2):245–253. doi: 10.1042/BJ20060749

Table 2. Kinetic parameters of wild-type and mutated enzymes in the directions of hydrolysis and synthesis.

Values in parentheses are percentage of wild-type. Truncation mutant p.W112stop is completely inactive. N/A, not assessed.

Enzymatic activity (μmol·min−1·mg−1)
Km (μM) Hydrolysis Hydrolysis Synthesis NAD/tetramer
Wild-type 15.09 0.748 (100%) 1.23 (100%) 3.5
p.Y143C 11.0 0.185 (25%) 0.42 (34%) 3.1
p.E115L 11.47 0.500 (68%) 0.75 (61%) 4.6
p.W112stop N/A N/A N/A N/A