In recent years, biocatalysis has emerged as a robust platform for synthesis. As a technology, it possesses distinct advantages that underline a powerful synthetic potential, such as operation under benign conditions, catalyst complementarity, excellent stereoselectivity and no requirements for protecting groups. This potential has been realized in no area more than the field of amine synthesis, where multiple reports describe the replacement of chemocatalytic pharmaceutical process methods with enzyme catalysed chemistry. While enzymes such as amine oxidases (MAOs) and imine reductases (IREDs) provide options for setting stereocentres in preformed N-heterocycles, cyclisation through N-alkylation by a single enzyme has been long unfeasible due to known options such as transaminases (TAs) and amine dehydrogenases (AmDHs) being limited solely to primary amination. In 2017, we reported the first example of an imine reductase capable of catalysing full aqueous reductive amination, and termed this sub-class "reductive aminases" (RedAms). Since then, the synthetic potential of these enzymes has been realized through industrial application in the synthesis of a drug candidate molecule on the process scale. The intrinsic condition complementarity of enzymes allows us to design biocatalytic syntheses in which multiple retrosynthetic steps are envisioned in one pot through cascade reactions. This has been exemplified in heterocycle synthesis, where we and others have demonstrated the ability of combined TA-IRED biocatalysis to generate saturated N-heterocycles from di-carbonyl substrates, which may be generated in situ through enzymatic redox manipulation. Further examples have seen IREDs applied to set stereocentres following cyclisation, with this approach finding expansion into chemoenzymatic synthesis through further organolithiummediated rearrangement to access 2,2-disubstituted N-heterocycles with stereocontrol. We have also previously demonstrated the application of RedAms in biocatalytic cascade reactions to achieve N-alkylation with redox surrogate reagents, firstly through a hydrogen borrowing approach and then followed by methodology that may utilize alcohols or carboxylic acid substrates through the use of an engineered alcohol oxidase (AcCO6) or carboxylic acid reductase (CARsr) respectively. In this work, we demonstrate an ability of RedAms to form Nheterocycles from dicarbonyl and amine substrates through sequential inter-intramolecular reductive amination, in the first report of this transformation.