Ontology highlight
ABSTRACT:
SUBMITTER: Ahmed FH
PROVIDER: S-EPMC5338246 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Ahmed F Hafna FH Mohamed A Elaaf AE Carr Paul D PD Lee Brendon M BM Condic-Jurkic Karmen K O'Mara Megan L ML Jackson Colin J CJ
Protein science : a publication of the Protein Society 20160717 9
Bilirubin is a potent antioxidant that is produced from the reduction of the heme degradation product biliverdin. In mammalian cells and Cyanobacteria, NADH/NADPH-dependent biliverdin reductases (BVRs) of the Rossmann-fold have been shown to catalyze this reaction. Here, we describe the characterization of Rv2074 from Mycobacterium tuberculosis, which belongs to a structurally and mechanistically distinct family of F420 H2 -dependent BVRs (F-BVRs) that are exclusively found in Actinobacteria. We ...[more]