EC Number   |
General Information |
Reference |
|---|
   1.14.99.48 | metabolism |
in the absence of heme, isoform IsdG is targeted for degradation by internally coded sequences. A flexible loop near the heme-binding pocket is required for IsdG degradation in the absence of heme. IsdG stability is increased by inhibiting ATPases |
-, 740051 |
| 1.14.99.48 | physiological function |
in the vertebrate host, Staphylococcus aureus fulfills its iron requirement by obtaining heme-iron from host hemoproteins via IsdG- and IsdI-mediated heme degradation. Isoforms IsdG and IsdI are structurally and mechanistically analogous but are differentially regulated by iron and heme availability |
-, 740051 |
| 1.14.99.48 | physiological function |
isoform IsdG-mediated heme catabolism enables the use of heme as a sole source of iron |
-, 725264 |
| 1.14.99.48 | physiological function |
isoform IsdI complements the heme utilization deficiency of a Corynebacterium ulcerans heme oxygenase mutant |
-, 725362 |
| 1.14.99.48 | physiological function |
isoforms IsdG and IsdI are both important for Staphylococcus aureus growth on haemin as a sole iron source and are necessary for full Staphylococcus aureus pathogenesis. Strains lacking IsdG, IsdI or both exhibit significantly impaired growth on hemin as a sole iron source when compared with wild-type. Inactivation of IsdG and IsdI in combination does not enhance the hemin utilization defect over that of either individual mutant strain. Overexpression of either IsdG or IsdI complements the loss of both enzymes, and expression of IsdG and IsdI is regulated by iron in a Fur-dependent manner and differentially regulated by iron and hemin |
-, 725994 |
| 1.14.99.48 | physiological function |
isoforms IsdG and IsdI are both important for Staphylococcus aureus growth on haemin as a sole iron source and are necessary for full Staphylococcus aureus pathogenesis. Strains lacking IsdG, IsdI or both exhibit significantly impaired growth on hemin as a sole iron source when compared with wild-type. Inactivation of IsdG and IsdI in combination does not enhance the hemin utilization defect over that of either individual mutant strain. Overexpression of either IsdG or IsdI complements the loss of both enzymes, and expression of IsdG and IsdI is regulated by iron in a Fur-dependent manner and differentially regulated by iron and hemin. Hemin-dependent upregulation of IsdG is occurring post-transcriptionally by enhancing its protein stability |
-, 725994 |
| 1.14.99.48 | physiological function |
oxidoreductase IruO, gene name thatNWMN2274, is the likely in vivo reductant required for heme degradation by Staphylococcus aureus. In the presence of NADPH and IruO, either IsdI or IsdG degrade bound heme 10fold more rapidly than with the chemical reductant ascorbic acid |
-, 725532 |
