Towards a general approach for tailoring the hydrophobic binding site of phenylalanine ammonia-lyases.

ABSTRACT: Unnatural substituted amino acids play an important role as chiral building blocks, especially for pharmaceutical industry, where the synthesis of chiral biologically active molecules still represents an open challenge. Recently, modification of the hydrophobic binding pocket of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) resulted in specifically tailored PcPAL variants, contributing to a rational design template for PAL-activity enhancements towards the differently substituted substrate analogues. Within this study we tested the general applicability of this rational design model in case of PALs, of different sources, such as from Arabidopsis thaliana (AtPAL) and Rhodosporidium toruloides (RtPAL). With some exceptions, the results support that the positions of substrate

SUBMITTER: Tork SD 

PROVIDER: S-EPMC9226071 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature