Table 2. Binding affinity and GH turnover number for C3larvinA and catalytic variants against NAD⁺.

Protein	KD (µM)1	kcat (min−1)1
C3larvinA	56 ± 11	261 (±20) × 10−3
C3larvinA AAA	34 ± 3	9.5 (±2) × 10−3
C3larvinA R105A	63 ± 13	5.3 (±0.1) × 10−3
C3larvinA AXA	143 ± 13	7.7 (±0.2) × 10−3

¹The measurements of the kinetic and substrate-binding affinity parameters for C3larvinA are described in the ‘Experimental procedures’ section. The parameters for NAD⁺ substrate binding and GH enzyme activity represent the mean ± SD of at least three different measurements.