Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution.

ABSTRACT: Transaminases are pyridoxal-5'-phosphate (PLP) binding enzymes, broadly studied for their potential industrial application. Their affinity for PLP has been related to their performance and operational stability and while significant differences in PLP requirements have been reported, the environment of the PLP-binding pocket is highly conserved. In this study, thorough analysis of the residue interaction network of three homologous transaminases Halomonas elongata (HeTA), Chromobacterium violaceum (CvTA), and Pseudomonas fluorescens (PfTA) revealed a single residue difference in their PLP binding pocket: an asparagine at position 120 in HeTA. N120 is suitably positioned to interact with an aspartic acid known to protonate the PLP pyridinium nitrogen, while the equivale

SUBMITTER: Roura Padrosa D 

PROVIDER: S-EPMC6813460 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature