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- W1825535009 endingPage "273102" @default.
- W1825535009 startingPage "273102" @default.
- W1825535009 abstract "The monooxygenase P450 BM-3 is a NADPH-dependent fatty acid hydroxylase enzyme isolated from soil bacterium Bacillus megaterium. As a pivotal member of cytochrome P450 superfamily, it has been intensely studied for the comprehension of structure-dynamics-function relationships in this class of enzymes. In addition, due to its peculiar properties, it is also a promising enzyme for biochemical and biomedical applications. However, despite the efforts, the full understanding of the enzyme structure and dynamics is not yet achieved. Computational studies, particularly molecular dynamics (MD) simulations, have importantly contributed to this endeavor by providing new insights at an atomic level regarding the correlations between structure, dynamics, and function of the protein. This topical review summarizes computational studies based on MD simulations of the cytochrome P450 BM-3 and gives an outlook on future directions." @default.
- W1825535009 created "2016-06-24" @default.
- W1825535009 creator A5068361493 @default.
- W1825535009 date "2015-06-10" @default.
- W1825535009 modified "2023-10-18" @default.
- W1825535009 title "Structure, dynamics, and function of the monooxygenase P450 BM-3: insights from computer simulations studies" @default.
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- W1825535009 doi "https://doi.org/10.1088/0953-8984/27/27/273102" @default.
- W1825535009 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26061496" @default.
- W1825535009 hasPublicationYear "2015" @default.
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