Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
| Autor: | Drew Tietz, Allison M. Colthart, Susan Sondej Pochapsky, Thomas C. Pochapsky |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Magnetic Resonance Spectroscopy Camphor 5-Monooxygenase Stereochemistry Protein Conformation lcsh:Medicine Stereoisomerism Substrate recognition Article Substrate Specificity 03 medical and health sciences Stereospecificity Protein structure Bacterial Proteins Cytochrome P-450 Enzyme System Catalytic Domain lcsh:Science chemistry.chemical_classification Multidisciplinary biology Chemistry lcsh:R Cytochrome P450 Nuclear magnetic resonance spectroscopy Monooxygenase Camphor 030104 developmental biology Enzyme biology.protein lcsh:Q Macrolides |
| Zdroj: | Scientific Reports Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017) |
| ISSN: | 2045-2322 |
| Popis: | Cytochrome P450 monooxygenases CYP101A1 and MycG catalyze regio- and stereospecific oxidations of their respective substrates, d-camphor and mycinamicin IV. Despite the low sequence homology between the two enzymes (29% identity) and differences in size and hydrophobicity of their substrates, the conformational changes that occur upon substrate binding in both enzymes as determined by solution NMR methods show some striking similarities. Many of the same secondary structural features in both enzymes are perturbed, suggesting the existence of a common mechanism for substrate binding and recognition in the P450 superfamily. |
| Databáze: | OpenAIRE |
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