A transaminase with β-activity from Variovorax boronicumulans for the production of enantiopure β-amino acids.

ABSTRACT: Enantioselective transamination of amino acids is a great challenge in biotechnology as suitable enzymes with wide substrate spectrum are rare. Here, we present a new transaminase from Variovorax boronicumulans (VboTA, Variovorax boronicumulansω-transaminase) which is specific for β-amino acids. The amino acid sequence of VboTA is similar to an ω-transaminase from Variovorax paradoxus, for which a crystal-structure is available. This similarity is allowing us to classify VboTA as a fold type 1 ω-transaminase (ω-TA). Although both enzymes have a high sequence similarity (86% identities, 92% positives), there are differences in the active center, which allow VboTA to accept a broader substrate spectrum. Both enzymes have also a different temperature stability and tempera

SUBMITTER: Wegner U 

PROVIDER: S-EPMC9850050 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature