Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1.

ABSTRACT: Many pathogenic bacteria can use heme compounds as a source of iron. Pathogenic Escherichia coli strains are capable of using hemoglobin as an iron source. However, the mechanism of heme acquisition from hemoglobin is not understood for this microorganism. We present the first molecular characterization of a hemoglobin protease (Hbp) from a human pathogenic E. coli strain. The enzyme also appeared to be a heme-binding protein. Affinity purification of this bifunctional protein enabled us to identify the extracellular gene product, and to clone and analyze its gene. A purification procedure developed for Hbp allowed us to perform functional studies. The protein interacted with hemoglobin, degraded it and subsequently bound the released heme. These results suggest that the protein is involve

SUBMITTER: Otto BR 

PROVIDER: S-EPMC2212542 | biostudies-literature | 1998 Sep

REPOSITORIES: biostudies-literature