Structural highlights
Function
CPXM_PRIMG Has the capacity to hydroxylate certain steroids in the 15-beta position. Also hydroxylates progesterone in the 11-alpha and 9-beta position.[1]
Publication Abstract from PubMed
CYP106A2 from Bacillus megaterium ATCC 13368 is known as a bacterial steroid hydroxylase which is also capable to hydroxylate a variety of terpenoids. To further analyze the substrate specificity of this enzyme, different resin acids of the abietane- and pimarane-type were tested towards binding and conversion. Product formation could be shown for all tested substrates. Spectroscopic studies revealed type-I binding spectra for isopimaric acid but dehydroabietic acid did not induce a high-spin shift of the enzyme. Interestingly, binding of abietic acid resulted in a type-II difference spectrum typical for nitrogenous inhibitors. Co-crystallization of CYP106A2 with abietic acid and structure determination revealed a bending of the heme-cofactor when abietic acid was bound in the active site. Quantum chemical calculations strongly suggest that this heme distortion is the cause of the unusual spectroscopic characteristics.
Crystal structure of CYP106A2 in substrate-free and substrate-bound form.,Janocha S, Carius Y, Hutter M, Lancaster CR, Bernhardt R Chembiochem. 2016 Feb 11. doi: 10.1002/cbic.201500524. PMID:26864272[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lisurek M, Simgen B, Antes I, Bernhardt R. Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation. Chembiochem. 2008 Jun 16;9(9):1439-49. doi: 10.1002/cbic.200700670. PMID:18481342 doi:http://dx.doi.org/10.1002/cbic.200700670
- ↑ Janocha S, Carius Y, Hutter M, Lancaster CR, Bernhardt R. Crystal structure of CYP106A2 in substrate-free and substrate-bound form. Chembiochem. 2016 Feb 11. doi: 10.1002/cbic.201500524. PMID:26864272 doi:http://dx.doi.org/10.1002/cbic.201500524
