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PMID:19091096
| Citation |
Guo, Y, Guo, G, Mao, X, Zhang, W, Xiao, J, Tong, W, Liu, T, Xiao, B, Liu, X, Feng, Y and Zou, Q (2008) Functional identification of HugZ, a heme oxygenase from Helicobacter pylori. BMC Microbiol. 8:226 |
|---|---|
| Abstract |
Iron is recognized as an important trace element, essential for most organisms including pathogenic bacteria. HugZ, a protein related to heme iron utilization, is involved in bacterial acquisition of iron from the host. We previously observed that a hugZ homologue is correlated with the adaptive colonization of Helicobacter pylori (H. pylori), a major gastro-enteric pathogen. However, its exact physiological role remains unclear. |
| Links |
PubMed PMC2644699 Online version:10.1186/1471-2180-8-226 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Gene Deletion; Gene Expression Regulation, Bacterial; Helicobacter pylori/enzymology; Helicobacter pylori/genetics; Helicobacter pylori/growth & development; Heme/metabolism; Heme Oxygenase (Decyclizing)/chemistry; Heme Oxygenase (Decyclizing)/genetics; Heme Oxygenase (Decyclizing)/metabolism; Hemin/metabolism; Humans; Iron/metabolism; Molecular Sequence Data; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Alignment |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004392: heme oxygenase (decyclizing) activity |
ECO:0000315: |
F |
Figures 4. No degradation of heme was observed in the absence of HugZ. Figures 5-6. Biliverdin and CO were produced by HugZ-catalyzed heme degradation. Thus, HugZ is a heme oxygenase. |
complete | ||||
| GO:0044444: cytoplasmic part |
ECO:0000314: |
C |
Figure 7B. Immunoelectron microscopy indicated HugZ located predominantly in the cytoplasm. |
complete | ||||
See also
References
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