Computational study on the polymerization reaction of d-aminopeptidase for the synthesis of d-peptides.

ABSTRACT: Almost all natural proteins are composed exclusively of l-amino acids, and this chirality influences their properties, functions, and selectivity. Proteases can recognize proteins composed of l-amino acids but display lower selectivity for their stereoisomers, d-amino acids. Taking this as an advantage, d-amino acids can be used to develop polypeptides or biobased materials with higher biostability. Chemoenzymatic peptide synthesis is a technique that uses proteases as biocatalysts to synthesize polypeptides, and d-stereospecific proteases can be used to synthesize polypeptides incorporating d-amino acids. However, engineered proteases with modified catalytic activities are required to allow the incorporation of d-amino acids with increased efficiency. To understand the stereospecificity p

SUBMITTER: Gimenez-Dejoz J 

PROVIDER: S-EPMC9053604 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature