3,4 Dihydroxy phenyl L-alanine (L-DOPA) is the gold standard Parkinson's disease therapy. A heme-dependent peroxidase (HDP) catalyzes the orrlio-hydroxylation of L-tyrosine to L-DOPA using H2O2 as the co-substrate. D-amino acid oxidase (DAAO) catalyzes the oxidative deamination of u-amino acids (e.g. o-alanine), and H2O2 is evolved. However, both the enzymes DAAO and HDP can be inactivated by H2O2 during the catalysis. In situ generation and utilization of H2O2 can siginificatly reduce the inactivation by H2O2. HDP exists as a monomer and DAAO is a dimeric enzyme. Herein, the C-terminus of HDP was specifically ligated to the N-terminus of the DAAO subunit with native peptide through the in vivo monomer-subunit splicing. In the splicing product HDP& DAAO, HDP is close to the DAAO subunit at a molecular distance, and the transfer of H2O2 from DAAO to HDP is facilitated. In addition, HDP&DAAO exhibited a higher stability than HDP. Kinetics analysis showed that both the substrates L-tyrosine and n-alanine obey the Michaelis-Menten kinetics. For the deamination of n-alanine, the catalytic efficiency of HDP&DAAO is 3.05 times that of DAAO. For the sybthesis of L-DOPA from L-tyrosine, the catalytic efficiency of HDP&DAAO is 1.58 times that of HDP. Furthermore, HDP&DAAO was encapsulated within a Znic-based coordination polymer (Zn-CP). The morphorogy of HDP&DAAO/Zn-CP can be regulated by the enzyme concentration, the catalytic efficiency of the conjugates was found to be dependent on the morphorogy. The conjugates HDP&DAAO/Zn-CP exhibited a higher catalytic efficiency than free HDP&DAAO.