Ontology highlight
ABSTRACT:
SUBMITTER: Schallmey A
PROVIDER: S-EPMC3036808 | biostudies-literature | 2011 Mar
REPOSITORIES: biostudies-literature
Schallmey Anett A den Besten Gijs G Teune Ite G P IG Kembaren Roga F RF Janssen Dick B DB
Applied microbiology and biotechnology 20101106 5
Cytochrome P450 monooxygenases are valuable biocatalysts due to their ability to hydroxylate unactivated carbon atoms using molecular oxygen. We have cloned the gene for a new cytochrome P450 monooxygenase, named CYP154H1, from the moderately thermophilic soil bacterium Thermobifida fusca. The enzyme was overexpressed in Escherichia coli at up to 14% of total soluble protein and purified to homogeneity in three steps. CYP154H1 activity was reconstituted using putidaredoxin reductase and putidare ...[more]