Two-substrate enzyme engineering using small libraries that combine the substrate preferences from two different variant lineages.

ABSTRACT: Improving the range of substrates accepted by enzymes with high catalytic activity remains an important goal for the industrialisation of biocatalysis. Many enzymes catalyse two-substrate reactions which increases the complexity in engineering them for the synthesis of alternative products. Often mutations are found independently that can improve the acceptance of alternatives to each of the two substrates. Ideally, we would be able to combine mutations identified for each of the two alternative substrates, and so reprogramme new enzyme variants that synthesise specific products from their respective two-substrate combinations. However, as we have previously observed for E. coli transketolase, the mutations that improved activity towards aromatic acceptor aldehydes, did not successfully re

SUBMITTER: Mukhopadhyay A 

PROVIDER: S-EPMC10787763 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature