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. 2006 Jul 27;398(Pt 1):37–43. doi: 10.1042/BJ20060274

Table 2. Kinetic parameters for the synthesis reactions of CgCBP with different glucosyl acceptors, and interactions in the complex structure.

The ΔΔG is the Gibbs energy of activation for kcat/Km for the enzymatic glucosyl transfer to an acceptor, relative to transfer to D-glucose, was calculated according to ΔΔG=RTln[(kcat/Km)D-glucose/(kcat/Km)acceptor], whereby R is 1.987 cal·mol−1·K−1 and T is 310.15 K [39]. Values in parentheses are taken from the results of CuCBP (T is 303.15 K) [32]. Values for 1,5-anhydroglucitol, isomaltose, gentiobiose and melibiose were determined in the present study.

Km (mM) kcat (s−1) kcat/Km (s−1·M−1) ΔΔG (kcal/mol) Hydrogen-bond pair Distance (Å)
Glucose [11] 2.1 98 46800
O-1 1,5-Anhydroglucitol 89 5.3 59 4.11 (>7) Glu649 Oϵ 2.6
O-2 Mannose [11] 115 39 342 3.03 (2.65) Tyr653 Oη 2.8
2-Deoxyglucose [11] 168 37 220 3.30 (2.24) Glu659 Oϵ1 3.0
Glucosamine [11] 13 15 1160 2.28 (2.19)
O-3 (3-Deoxyglucose) (4.01) Lys658 Nζ 3.0
Glu659 Oϵ2 2.7
O-4 Asp490 Oδ 2.6
O-5 5a-Carba-β-D-glucopyranose [12] 55 93 1680 2.05 Gln165
(other monomer) Nϵ 3.2
O-6 6-Deoxyglucose [11] 24 139 5780 1.29 (0.77) None
Xylose [11] 84 31 372 2.98 (2.15)
Isomaltose 71 1.9 27
Gentiobiose 83 7.2 87
Melibiose 93 2.3 24