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A possible (and widely accepted) explanation is that these ancestral enzymes possessed broad substrate specificity, allowing them to catalyze several different chemical reactions (see below).
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The use of a protease with broad substrate specificity, such as thermolysin allows the identification of cleavage sites solely on the basis of the flexibility of the protein substrate.
These rather general criteria allow AcrB to accommodate a broad substrate specificity, e.g., that observed in multidrug resistance (Yamaguchi et al. 2015).
Some of these enzymes are specific and some have broad substrate specificity.
This approach allowed us to successfully identify GH1 enzymes with sought-after specifications, notably activity at high temperatures in the presence of IL, broad substrate specificity, and activity against more complex substrates such as laminarin, that are potentially useful in a biotechnological setting.
Together, these molecules efficiently generate plasmin, a serine protease with broad substrate specificity.
In addition, the Fe-type NHase exhibited broad substrate specificity.
The enzyme furthermore had a unusual broad substrate specificity, including U, 5-HmU, 5-FU and εC.
Threonine-peptidases of the T1-family are multi-subunit complexes with broad substrate specificity.
Furthermore, Streptomyces PLDs present advantages related to their broad substrate specificity and ease of enzyme preparation.
Human carboxylesterase 1 (hCexhibitsbroadbroad substrate specificity and is involved in xenobiotic processing and endobiotic metabolism.
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