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. Author manuscript; available in PMC: 2013 Aug 14.
Published in final edited form as: Biochemistry. 2012 Jul 31;51(32):6463–6475. doi: 10.1021/bi300811t

Table 6.

Kinetic constants for hydrolysis of GB, GD and GFa.

Enzyme Substrate kcat (s−1) Km (μM) kcat/Km (M−1 s−1)
Wild-type GB 430 ± 50 1800 ± 400 2.4 (0.6) × 105
Wild-type GD 12 ± 1 800 ± 200 1.5 (0.4) × 104
Wild-type GF 210 ± 30 900 ± 300 2.3 (0.8) × 105
YT GB 520 ± 30 260 ± 50 2.0 (0.4) × 106
YT GD 240 ± 20 460 ± 90 5 (1) × 105
YT GF 130 ± 10 170 ± 50 8 (2) × 105
YTRN GD 100 ± 10 300 ± 100 4 (2) × 105
a

Racemic mixtures of GB, GD, and GF were used for these measurements.