Ontology highlight
ABSTRACT:
SUBMITTER: Zamocky M
PROVIDER: S-EPMC3442556 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Zámocký Marcel M García-Fernández Queralt Q Gasselhuber Bernhard B Jakopitsch Christa C Furtmüller Paul G PG Loewen Peter C PC Fita Ignacio I Obinger Christian C Carpena Xavi X
The Journal of biological chemistry 20120720 38
Catalase-peroxidases (KatGs) are bifunctional heme enzymes widely spread in archaea, bacteria, and lower eukaryotes. Here we present the first crystal structure (1.55 Å resolution) of an eukaryotic KatG, the extracellular or secreted enzyme from the phytopathogenic fungus Magnaporthe grisea. The heme cavity of the homodimeric enzyme is similar to prokaryotic KatGs including the unique distal (+)Met-Tyr-Trp adduct (where the Trp is further modified by peroxidation) and its associated mobile argin ...[more]