Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.

ABSTRACT: One of the main factors hampering the implementation in industry of transaminase-based processes for the synthesis of enantiopure amines is their often low storage and operational stability. Our still limited understanding of the inactivation processes undermining the stability of wild-type transaminases represents an obstacle to improving their stability through enzyme engineering. In this paper we present a model describing the inactivation process of the well-characterized (S)-selective amine transaminase from Chromobacterium violaceum. The cornerstone of the model, supported by structural, computational, mutagenesis and biophysical data, is the central role of the catalytic lysine as a conformational switch. Upon breakage of the lysine-PLP Schiff base, the strain associated with the ca

SUBMITTER: Ruggieri F 

PROVIDER: S-EPMC6861513 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature