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The Rhodococcus genus exhibits diverse enzymatic activity that can be exploited in the conversion of natural and anthropogenic nitrogenous compounds. This catalytic response provides a selective advantage in terms of available nutrients while also serving to remove otherwise harmful xenobiotics. This review provides a critical assessment of the literature on bioconversion of organonitrogen compounds with a consideration of applications in bioremediation and commercial biotechnology. By examining the major nitro-organic compounds (amino acids, amines, nitriles, amides and nitroaromatics) in turn, the considerable repertoire of Rhodococcus spp. is established. The available published enzyme reaction data is coupled with genomic characterisation to provide a molecular basis for Rhodococcus enzyme activity with an assessment of the cellular properties that aid substrate accessibility and ensure stability. The metabolic gene clusters associated with the observed reaction pathways are identified and future directions in enzyme optimisation and metabolic engineering are assessed.Alanine dehydrogenase (RHA1_ro01495, ald1, ald2) and aspartate ammonia lyase (aspA1, aspA2, aspA3), with corresponding transaminases, provide alternative ping-pong (bi-bi) systems. Specificity and cellular catalytic efficiency is extended by a number of genes encoding asparagine dehydrogenase, arginine, cysteine, histidine and serine ammonia lyase ( Table 2). The production of