Ontology highlight
ABSTRACT:
SUBMITTER: Durand F
PROVIDER: S-EPMC3724473 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Durand Fabien F Kjaergaard Christian Hauge CH Suraniti Emmanuel E Gounel Sébastien S Hadt Ryan G RG Solomon Edward I EI Mano Nicolas N
Biosensors & bioelectronics 20120225 1
A CotA multicopper oxidase (MCO) from Bacillus pumilus, previously identified as a laccase, has been studied and characterized as a new bacterial bilirubin oxidase (BOD). The 59 kDa protein containing four coppers, was successfully over-expressed in Escherichia coli and purified to homogeneity in one step. This 509 amino-acid enzyme, having 67% and 26% sequence identity with CotA from Bacillus subtilis and BOD from Myrothecium verrucaria, respectively, shows higher turnover activity towards bili ...[more]