Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 501, Issue 4, Pages 846-850Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.05.014
Keywords
CYP; Biocatalysis; C-H activation; Crystallography; Hydroxylation
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Funding
- European Union's Seventh Framework Programme for research, technological development and demonstration [613849]
- European Union's Horizon 2020 Programme for research and innovation actions [H2020-LEIT BIO-2014-1, 635734]
- BBSRC [BB/M017702/1] Funding Source: UKRI
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The first crystal structure of a class VII P450, CYP1161346 from Tepidiphilus thermophilus, has been solved at 1.9 angstrom resolution. The structure reveals overall conservation of the P450-fold and a water conduit around the I-helix. Active site residues have been identified and sequence comparisons have been made with other class VII enzymes. A structure similarity search demonstrated that the P450-TT structure is similar to enzymes capable of oxy-functionalization of fatty acids, terpenes, macrolides, steroids and statins. The insight gained from solving this structure will provide a guideline for future engineering and modelling studies on this catalytically promiscuous class of enzymes. (C) 2018 Elsevier Inc. All rights reserved.
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