Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese.
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Purified HemF is an O2-dependent, manganese-stimulated coproporphyrinogen III oxidase.
"Molecular oxygen is essential for the enzymatic reaction."
Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation.
Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant.
The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress.
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hemF is OxyR-induced and required for heme synthesis and H2O2 tolerance during peroxide stress.
"These data all indicate that during H2O2 stress the induced mangano-enzyme HemF becomes the critical coproporphyrinogen III oxidase."
Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry P36553 (HEM6_ECOLI)
Curation notes for E. coli hemF