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The hydrogen bonds (i.e., the enthalpy term in ∆G L or ∆G R) contribute favorably to both substrate affinity and selectivity.
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Kinetic studies indicated that the cofactor modification increased the substrate affinity and catalytic efficiency both in aqueous buffer and some organic solvents.
Kinetic studies further demonstrated differential substrate affinity and catalytic efficiency among the SULT1A3 allozymes.
Moreover, all of the mutants showed greater substrate affinity and kcat/Km than the native Srxyn.
The models could be used to identify amino acids for each P′ substrate position that are favorable for, respectively, high substrate affinity and cleavage rate.
Therefore, substrate affinity and regiospecificity of an O-methyltransferase in vivo and in vitro can be controlled by cleavage of an N-terminal domain.
This indicates that the substrate affinity and catalytic activity is inhibited by LysoPC.
Enzyme activity is dependent on the substrate affinity and the conversion efficiency of the active centre.
Immobilization also enhanced the substrate affinity and catalytic efficiency of LiP as evidenced by lower Km and high Vmax values.
All UGE isoenzymes can interconvert UDP-Glc and UDP-Gal in vitro, although they show differences in the substrate affinity and reaction requirements [ 9, 11].
The lower value of Km and higher Vmax values for immobilized enzyme indicated that immobilization enhanced the substrate affinity and catalytic efficiency of LiP.
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