Characterization of proteins from the 3N5M family reveals an operationally stable amine transaminase.

ABSTRACT: Amine transaminases (ATA) convert ketones into optically active amines and are used to prepare active pharmaceutical ingredients and building blocks. Novel ATA can be identified in protein databases due to the extensive knowledge of sequence-function relationships. However, predicting thermo- and operational stability from the amino acid sequence is a persisting challenge and a vital step towards identifying efficient ATA biocatalysts for industrial applications. In this study, we performed a database mining and characterized selected putative enzymes of the β-alanine:pyruvate transaminase cluster (3N5M) - a subfamily with so far only a few described members, whose tetrameric structure was suggested to positively affect operational stability. Four putative transaminases (TA-1: Bilophilia w

SUBMITTER: Kollipara M 

PROVIDER: S-EPMC9418295 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature