Caenorhabditis elegans and human dual oxidase 1 (DUOX1) "peroxidase" domains: insights into heme binding and catalytic activity.

ABSTRACT: The seven members of the NOX/DUOX family are responsible for generation of the superoxide and H(2)O(2) required for a variety of host defense and cell signaling functions in nonphagocytic cells. Two members, the dual oxidase isozymes DUOX1 and DUOX2, share a structurally unique feature: an N-terminal peroxidase-like domain. Despite sequence similarity to the mammalian peroxidases, the absence of key active site residues makes their binding of heme and their catalytic function uncertain. To explore this domain we have expressed in a baculovirus system and purified the Caenorhabditis elegans (CeDUOX1(1-589)) and human (hDUOX1(1-593)) DUOX1 "peroxidase" domains. Evaluation of these proteins demonstrated that the isolated hDUOX1(1-593) does not bind heme and has no intrinsic peroxidase activit

SUBMITTER: Meitzler JL 

PROVIDER: S-EPMC2707201 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature