Coupled Natural Fusion Enzymes in a Novel Biocatalytic Cascade Convert Fatty Acids to Amines.

ABSTRACT: Tambjamine YP1 is a pyrrole-containing natural product. Analysis of the enzymes encoded in the Pseudoalteromonas tunicata "tam" biosynthetic gene cluster (BGC) identified a unique di-domain biocatalyst (PtTamH). Sequence and bioinformatic analysis predicts that PtTamH comprises an N-terminal, pyridoxal 5'-phosphate (PLP)-dependent transaminase (TA) domain fused to a NADH-dependent C-terminal thioester reductase (TR) domain. Spectroscopic and chemical analysis revealed that the TA domain binds PLP, utilizes l-Glu as an amine donor, accepts a range of fatty aldehydes (C₇-C₁₄ with a preference for C₁₂), and produces the corresponding amines. The previously characterized PtTamA from the "tam" BGC is an ATP-dependent, di-domain

SUBMITTER: Richardson SM 

PROVIDER: S-EPMC9594044 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature