Ontology highlight
ABSTRACT:
SUBMITTER: Sugadev R
PROVIDER: S-EPMC3180034 | biostudies-literature | 2011
REPOSITORIES: biostudies-literature
Sugadev Ragumani R Ponnuswamy M N MN Sekar K K
International journal of biochemistry and molecular biology 20110129 1
To study the functional role of NADPH during mammalian catalase inhibition, the X-ray crystal structures of NADPH-depleted bovine liver catalase and its inhibitor complexes, cyanide and azide, determined at 2.8Å resolution. From the complex structures it is observed that subunits with and without an inhibitor/catalytic water molecule are linked by N-terminal domain swapping. Comparing mammalian- and fungal- catalases, we speculate that NADPH-depleted mammalian catalases may function as a domain- ...[more]