A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild
| Autor: | Yihao Zhuang, Alexander E. Ferrazzoli, Nathan R. Wong, Jeffrey Futcher, Jeffrey M. Matthews, Thomas C. Pochapsky, Deani L. Cooper, Xinyue Liu, Hannah Lloyd, Theodore M. Pochapsky, Phillix Esquea, Allison M. Colthart |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Oxidative phosphorylation Biochemistry Article Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Cytochrome P-450 Enzyme System Pseudomonas Gene Ferredoxin Soil Microbiology chemistry.chemical_classification Limonene biology Shotgun sequencing Chemistry Terpenes Cytochrome P450 Pseudomonas nitroreducens biology.organism_classification 030104 developmental biology Enzyme biology.protein |
| Zdroj: | Journal of inorganic biochemistry. 188 |
| ISSN: | 1873-3344 |
| Popis: | A strategy for elucidating sequence determinants of function in the class of cytochrome P450 (CYP) enzymes that catalyze the first steps of terpene metabolism in wild microbiomes is described. Wild organisms that can use camphor, terpineol, pinene and limonene were isolated from soils rich in coniferous waste. Cell free extracts and growth beers were analyzed by gas chromatography/mass spectrometry to identify primary oxidative metabolites. For one organism, Pseudomonas nitroreducens TPJM, a cytochrome P450 (CYP108B1) isolated from cell free extracts was demonstrated to catalyze the oxidation of α-terpineol in assays combining the native ferredoxin and putidaredoxin reductase, and the resulting oxidation products identified by gas chromatography/mass spectrometry. Shotgun sequencing of PnTPJM identified four candidate P450 genes, including an apparently fragmentary gene with a high degree of homology with the known enzyme CYP108 (P450terp). |
| Databáze: | OpenAIRE |
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