The very first examples of enzyme-DNA-inorganic materials will be presented. DNA improved the bound enzyme behavior and these novel biocatalytic nanomaterials will be discussed in some detail. The layered inorganic solid, alpha-Zr(IV) phosphate (alpha-Zr(HPO4)2.H2O, abbreviated as alpha-ZrP) serves as an excellent host to accommodate both the enzyme and the nucleic acid, and the binding has been carried out under benign ambient conditions (aqueous solutions at room temperature and neutral pH. Binding of DNA to alpha-ZrP is promoted by the enzyme, and DNA binding did not occur in the absence of the enzyme. In earlier studies, we demonstrated the binding of several proteins and enzymes in the galleries of alpha-ZrP and binding resulted in the retention of protein structure to a significant extent. Bound enzymes demonstrated activities that are comparable to those in solution, and in specific cases we noted activities better than in solution. Intercalation of DNA along with the proteins, for example, met-hemoglobin (Hb) or met-myoglobin (Mb) indicated improved protein structure. The protein/DNA/alpha-ZrP materials have been characterized by XRD, SEM, TEM, ITC, DSC and circular dichroism studies. The peroxidase-like activity of bound Hb is enhanced five-fold when DNA is co-immobilized. Improved structure and enhanced activities are welcome changes for biocatalytic applications and the strong role of DNA in enhancing bound protein properties is novel. This study provides a simple method for binding of DNA to negatively charged solids, and such approaches aid in engineering more effective synthetic materials for gene delivery and drug-delivery applications.