Structure and Mutation of the Native Amine Dehydrogenase MATOUAmDH2.

ABSTRACT: Native amine dehydrogenases (nat-AmDHs) have recently emerged as a potentially valuable new reservoir of enzymes for the sustainable and selective synthesis of chiral amines, catalyzing the NAD(P)H-dependent ammoniation of carbonyl compounds with high activity and selectivity. MATOUAmDH2, recently identified from the Marine Atlas of Tara Oceans Unigenes (MATOUv1) database of eukaryotic genes, displays exceptional catalytic performance against its best identified substrate, isobutyraldehyde, as well as having broader substrate scope than other nat-AmDHs. In the interests of providing a platform for the rational engineering of this and other nat-AmDHs, we have determined the structure of MATOUAmDH2 in complex with NADP⁺ and also with the cofactor and cyclohexylamine. Monomers with

SUBMITTER: Bennett M 

PROVIDER: S-EPMC9325545 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature