7DI3
Cytochrome P450 (CYP105D18) W.T.
Summary for 7DI3
| Entry DOI | 10.2210/pdb7di3/pdb |
| Descriptor | Cytochrome P450 hydroxylase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | papaverine n-oxide, eukaryotic cytochrome p450, chemical modification, heme oxidation, transferase |
| Biological source | Streptomyces laurentii |
| Total number of polymer chains | 1 |
| Total formula weight | 45019.75 |
| Authors | |
| Primary citation | Pardhe, B.D.,Do, H.,Jeong, C.S.,Kim, K.H.,Lee, J.H.,Oh, T.J. Characterization of high-H 2 O 2 -tolerant bacterial cytochrome P450 CYP105D18: insights into papaverine N-oxidation. Iucrj, 8:684-694, 2021 Cited by PubMed Abstract: The bacterial CYP105 family is involved in secondary metabolite biosynthetic pathways and plays essential roles in the biotransformation of xenobiotics. This study investigates the newly identified HO-mediated CYP105D18 from as the first bacterial CYP for N-oxidation. The catalytic efficiency of CYP105D18 for papaverine N-oxidation was 1.43 s µ . The heme oxidation rate () was low (<0.3 min) in the presence of 200 m HO. This high HO tolerance capacity of CYP105D18 led to higher turnover prior to heme oxidation. Additionally, the high-resolution papaverine complexed structure and substrate-free structure of CYP105D18 were determined. Structural analysis and activity assay results revealed that CYP105D18 had a strong substrate preference for papaverine because of its bendable structure. These findings establish a basis for biotechnological applications of CYP105D18 in the pharmaceutical and medicinal industries. PubMed: 34258016DOI: 10.1107/S2052252521005522 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
Download full validation report
