Ontology highlight
ABSTRACT:
SUBMITTER: Matsui T
PROVIDER: S-EPMC3672231 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature
Biochemistry 20130424 18
IsdG and IsdI from Staphylococcus aureus are novel heme-degrading enzymes containing unusually nonplanar (ruffled) heme. While canonical heme-degrading enzymes, heme oxygenases, catalyze heme degradation coupled with the release of CO, in this study we demonstrate that the primary C1 product of the S. aureus enzymes is formaldehyde. This finding clearly reveals that both IsdG and IsdI degrade heme by an unusual mechanism distinct from the well-characterized heme oxygenase mechanism as recently p ...[more]