Structure of AlkB–AlkG shows details of alkane terminal C–H selectivity and functionalization
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
https://www.nature.com/articles/s41594-023-00964-2.pdf
Reference5 articles.
1. Labinger, J. A. & Bercaw, J. E. Understanding and exploiting C–H bond activation. Nature 417, 507–514 (2002). A review article that presents the challenges and opportunities of selective C–H bond activation.
2. Bordeaux, M., Galarneau, A. & Drone, J. Catalytic, mild, and selective oxyfunctionalization of linear alkanes: current challenges. Angew. Chem. Int. Ed. 51, 10712–10723 (2012). A review article that presents promising chemical and biological catalysts for alkane oxidation.
3. Koch, D. J., Chen, M. M., van Beilen, J. B. & Arnold, F. H. In vivo evolution of butane oxidation by terminal alkane hydroxylases AlkB and CYP153A6. Appl. Environ. Microbiol. 75, 337–344 (2009). This paper reports the use of the directed evolution of AlkB for butane oxidation.
4. Shanklin, J., Whittle, E. & Brian, G. F. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry 33, 12787–12794 (1994). This paper identified a histidine motif present in desaturases and related enzymes that is necessary for catalysis in desaturases.
5. Shanklin, J. & Whittle, E. Evidence linking the Pseudomonas oleovorans alkane ω-hydroxylase, an integral membrane diiron enzyme, and the fatty acid desaturase family. FEBS Lett. 545, 188–192 (2003). This paper demonstrated that the histidine residues that AlkB and desaturase enzymes have in common are necessary for AlkB activity.
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