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We sought to explore the sequence basis of substrate differences using a phylogeny-based design of site-directed mutations.
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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 ].
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].
Nitrilases have been classified into three major categories on the basis of substrate specificity, although some nitrilases exhibit broad substrate specificity.
On the basis of substrate specificity, they are classified as serine/threonine, tyrosine, dual specificity, or histidine protein phosphatases.
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