Characterization of high-H2O2-tolerant bacterial cytochrome P450 CYP105D18: insights into papaverine N-oxidation
| Autor: | Chang-Sook Jeong, Bashu Dev Pardhe, Hackwon Do, Jun Hyuck Lee, Ki-Hwa Kim, Tae-Jin Oh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Streptomyces laurentii
Heme oxidation Secondary metabolite 01 natural sciences Biochemistry 03 medical and health sciences chemistry.chemical_compound enzyme mechanisms Biotransformation CYP105D18 medicine General Materials Science 030304 developmental biology 0303 health sciences Papaverine Crystallography biology 010405 organic chemistry papaverine N-oxide Cytochrome P450 Substrate (chemistry) General Chemistry H2O2 tolerance Condensed Matter Physics Research Papers 0104 chemical sciences chemistry co-crystals QD901-999 biology.protein Xenobiotic crystal morphology medicine.drug |
| Zdroj: | IUCrJ IUCrJ, Vol 8, Iss 4, Pp 684-694 (2021) |
| ISSN: | 2052-2525 |
| Popis: | The crystal structure of CYP105D18 and its unique structural features for papaverine N-oxidation are presented. 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 H2O2-mediated CYP105D18 from Streptomyces laurentii as the first bacterial CYP for N-oxidation. The catalytic efficiency of CYP105D18 for papaverine N-oxidation was 1.43 s−1 µM −1. The heme oxidation rate (k) was low ( |
| Databáze: | OpenAIRE |
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