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Given that the substrate is specifically designed on the basis of the natural substrate, substrate and stereoselectivity is ensured due to nearly identical steric properties.
β-Glucosidases may be classified into three groups on the basis of substrate specificity.
Although Km varies ∼1000-fold ∼1000-foldcacrossthe molaccasesbasis of substhete binding is poorly understood.
Species-specific modules were divided into two main categories on the basis of substrate type tested: substrate A and substrate B. In summary, six modules per species contained substrate A and six modules were filled with substrate B [ see Supporting Information ].
Nitrilases have been classified into three major categories on the basis of substrate specificity, although some nitrilases exhibit broad substrate specificity.
These results offer insights into the molecular basis of substrate recognition for the BmaI1 enzyme.
The molecular basis of substrate selectivity in AHL synthases, however, remains poorly understood.
Such interactions could constitute the basis of substrate specificity in hOGA.
However, the mechanism of action and the structural basis of substrate specificity of rhomboids remain unresolved, largely due to the absence of structural analyses of rhomboid substrate complexes.
The structural basis of substrate recognition is mainly determined by post-translational modification of short epitopes (degrons) of the substrate, e.g. phosphorylation, hydroxylation or glycosylation [ 28].
On the basis of this presumed substrate binding mode, we sought residues that might control the stereoselectivity of OYE 2.6 by direct interactions with the substrate.
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