Metal centers coordinated within protein environments underpin the efficiency and specificity of natural enzymes, yet their complexity and fragility limit broader catalytic applications. Bioinspired minimalistic alternatives that integrate molecular self-assembly with metal coordination offer a promising route toward robust, enzyme-like systems. Here, we report a single-step, atom-economic synthesis of a copper–tyrosine (CuY) supramolecular assembly that functions as a minimalist bionanozyme. Structural and morphological analyses reveal the formation of an ordered, nanotubular, self-assembled architecture, confirmed by XRD, SAXS, FTIR, TGA, MS, and XPS, and supported by DFT calculations. The CuY assembly exhibits pronounced peroxidase-like activity toward o-phenylenediamine, with kinetic parameters quantitatively extracted using Michaelis–Menten analysis. Importantly, we demonstrated that the catalytic performance is not solely dictated by copper coordination but is strongly regulated by the dynamic self-assembled state of the CuY network. We showed that the coordination-driven remodelling of tyrosine assemblies induces a nonlinear modulation of catalytic activity, revealing a direct coupling between supramolecular organisation and enzyme-like function. This work represents the first report of enzyme-mimetic catalysis arising from a tyrosine based single amino acid–metal coordination system and highlights molecular self-assembly as a central regulatory element in minimalist catalytic networks. Our findings provide new insights into the design of life-like catalytic materials based on metal–amino acid assemblies.