The well studied bacterial tyrosinases from the Streptomyces sp. bacteria are distinguishable from their eukaryotic counterparts by the absence of a C-terminal extension. In the present study, we report that the tyrosinase from the bacterium also has such a C-terminal extension, thus making it distinct from the Verrucomicrobium spinosumStreptomyces enzymes. The entire tyrosinase gene from V. spinosum codes for a 57 kDa protein (full-length unprocessed form), which has a twin arginine translocase type signal peptide, the two copper-binding motifs typical of the tyrosinase protein family and the aforementioned C-terminal extension. We expressed various mutants of the recombinant enzyme in Escherichia coli and found that removal of the C-terminal extension by genetic engineering or limited trypsin digest of the pro-form results in a more active enzyme (i.e. 30–100-fold increase in monophenolase and diphenolase activities). Further studies also revealed the importance of a phenylalanine residue in this C-terminal domain. These results demonstrate that the V. spinosum tyrosinase is a new example of this interesting family of enzymes. In addition, we show that this enzyme can be readily overproduced and purified and that it will prove useful in furthering the understanding of these enzymes, as well as their biotechnological application.