Amine transaminases (ATAs) propose an appealing alternative to transition metal catalysts as they can provide chiral amines of high purity from pro-chiral compounds by asymmetric synthesis. Industrial interest on ATAs arises from the fact that chiral amines are present in a wide spectrum of pharmaceutical and other high value-added chiral compounds and building blocks. Despite their potential as useful synthetic tools, several drawbacks such as challenges associated with the thermodynamic equilibrium can still impede their utilization. Several methods have been developed to displace the equilibrium, such as the use of alanine as an amine donor and the subsequent removal of pyruvate with a two-enzyme system, or the use of o-xylylene diamine. To date, the preferred amine donor remains isopropylamine (IPA), as the produced acetone can be removed easily under low pressure or slight heating, without complicating the process with other enzymes. Despite its small size, IPA is not widely accepted from wild-type ATAs, and this fact compromises its wide applicability. Herein, we index the reported biocatalytic aminations with IPA, comparing the sequences, while we discuss significant parameters of the process, such as the effect of temperature and pH, as well as the protein engineering and process development advances in the field. This information is expected to provide an insight for potential designs of tailor-made ATAs and IPA processes.