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The presence of different possible substrate-binding domains confers the great substrate specificity and selectivity of UGT proteins, together with their broad tissue expression profiles.
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These complexes can associate with different regulatory subunits, which act as substrate-specific adaptor proteins providing for even greater substrate specificity.
However, they have a great diversity in substrate specificity.
As mutational events occurred leading to greater degrees of substrate specificity, the dimeric phosphagen kinases became evolutionary separated such that the substrate specificity could not be interchanged by a small number of mutations.
Moreover, several positively selected amino acids were located in specific regions known to be of great functional significance for the substrate specificity and enzymatic activity of type-A feruloyl esterases and lipases.
Of greatest interest is the argument that enzymes catalyzing coupled vectorial processes must undergo large changes in substrate specificity associated with different conformational states.
This approach outlines a general method of great potential for fine-tuning substrate specificity and tailoring stereoselectivity of recombinant enzymes.
Members of the CYP2C enzyme subfamily exhibit the greatest species differences in expression, substrate specificity, and regulation compared to other CYP subfamilies involved in the metabolism and bioactivation of xenobiotics (Mugford and Kedderis, 1998; Tsao et al., 2001; Waxman and Holloway, 2009).
The broad substrate specificity, biochemical stability, and great synergistic effect with xylanase make Ac-Abf51A a potentially interesting enzyme for application in industrial biomass degradation.
Thr 134 and His 157 are therefore likely to be of great importance in substrate recognition and in defining substrate specificity at the S1 site.
CLIP-tag with potent catalytic activity exhibited a 105-fold change in substrate specificity and a 100-fold greater preference for BC over BG [259].
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