1 research outputs found
Monobody-Mediated Alteration of Lipase Substrate Specificity
Controlling the catalytic
properties of enzymes remain an important
challenge in chemistry and biotechnology. We have recently established
a strategy for altering enzyme specificity in which the addition of
proxy monobodies, synthetic binding proteins, modulates the specificity
of an otherwise unmodified enzyme. Here, in order to examine its broader
applicability, we employed the strategy on <i>Candida rugosa</i> lipase 1 (CRL1), an enzyme with a tunnel-like substrate binding
site. We successfully identified proxy monobodies that restricted
the substrate specificity of CRL1 toward short-chain fatty acids.
The successes with this enzyme system and a β-galactosidase
used in the previous work suggest that our strategy can be applied
to diverse enzymes with distinct architectures of substrate binding
sites