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. Author manuscript; available in PMC: 2024 Apr 18.
Published in final edited form as: Methods Enzymol. 2023 Apr 18;685:95–126. doi: 10.1016/bs.mie.2023.03.002

Table 2.

Intrinsic Phosphodianion Binding Energies for Wildtype and Variant Forms of OMPDC and the Effects of these Amino Acid Substitutions on the Intrinsic Phosphodianion Binding Energy GPi (eq 1).a

OMPDC (kcat/Km )SPikcat/KSH (eq 1) GPi (kcal/mol) eq 1 (GPi)WT(GPi)Var (kcal/mol)
Wild type 4.2 x 108 11.7
Q215A 2.3 x 107 10.0 1.7
Y217F 1.5 x 107 9.8 1.9
R235A 3.5 x 104 6.2 5.5
Q215A/Y217F 7.4 x 105 8.0 3.7
Q215A/ R235A 3300 4.8 6.9
Y217F /R235A 410 3.6 8.1
Q215A/Y217F/R235A 12 1.5 10.2
a

Data from [54].