Transaminases are highly versatile biocatalysts, shuttling amine groups between donors (primary amines) and acceptors (aldehydes and ketones) using a PLP, pyridoxal-5-phosphate, cofactor. The versatility of transaminases is well recognised, and the enzymes have applications in specific areas of the chemical industry. However, for a large number of processes, conventional chemical methods are still utilised. Recently we identified a Pseudomonas species (Pseudomonas sp. strain AAC) which has the capacity to use 12-aminododecanoic acid, the constituent building block of homo-Nylon-12, as a sole nitrogen source. Growth of Pseudomonas sp. strain AAC could also be supported using a range of additional omega-amino alkanoates. This metabolic function was shown to likely be dependent upon one or more transaminases (TAs). Genes encoding putative transaminases were identified from the genome of Pseudomonas sp. AAC and each of the genes was cloned, expressed in E. coli and tested for activity. In addition, an attempt to characterize the enzymes and identify their physiological functions was made. The results of these investigations, as well as the industrial applications of the transaminases will be discussed.