Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.

ABSTRACT: Transaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates for a broad range of drugs and fine chemicals. Here, we describe the discovery and characterisation of new transaminases from microorganisms which were enriched in selective media containing (R)-amines as sole nitrogen source. While most of the candidate proteins were clearly assigned to known subgroups of the fold IV family of PLP-dependent enzymes by sequence analysis and characterisation of their substrate specificity, some of them did not fit to any of these groups. The structure of one of these enzymes from Curtobacterium pusillum, which can convert d-amino acids and various (R)-amines with high enantioselectivity, was solved at a resolution of 2.4 Å. It shows significant differe

SUBMITTER: Pavkov-Keller T 

PROVIDER: S-EPMC5131300 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature