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Substrate recognition by two different P450s: Evidence for conserved roles in a common fold.
- Source :
-
Scientific reports [Sci Rep] 2017 Oct 19; Vol. 7 (1), pp. 13581. Date of Electronic Publication: 2017 Oct 19. - Publication Year :
- 2017
-
Abstract
- 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.
- Subjects :
- Camphor chemistry
Camphor metabolism
Catalytic Domain
Macrolides chemistry
Macrolides metabolism
Magnetic Resonance Spectroscopy
Protein Conformation
Stereoisomerism
Substrate Specificity
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Camphor 5-Monooxygenase chemistry
Camphor 5-Monooxygenase metabolism
Cytochrome P-450 Enzyme System chemistry
Cytochrome P-450 Enzyme System metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 7
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 29051575
- Full Text :
- https://doi.org/10.1038/s41598-017-14011-w