EC Number   |
General Information |
Reference |
|---|
    1.16.3.1 | evolution |
enzyme HP-NAP belongs to the DNA-protecting proteins under starved conditions (Dps) family, which has significant structural similarities to the dodecameric ferritin family. The overall structure of HP-NAP YS39 is similar to those of other HP-NAPs and Dps proteins |
-, 744474 |
| 1.16.3.1 | evolution |
in addition to the classical classification, another cluster containing AaMco1 and filamentous ascomycete hypothetical proteins, putative multicopper oxidases (MCOs) or proteins called ascorbate oxidases is identified on the basis of sequence similarity. This group is named ascomycete MCOs. Neighbor joining tree of multicopper oxidase amino acid sequences, phylogenetic analysis, overview |
-, 744437 |
| 1.16.3.1 | evolution |
the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture |
745442 |
| 1.16.3.1 | malfunction |
cytosolic FOX activity increases 30% in iron-deficient rats (compared with controls) but is unchanged in copper-deficient rats |
728682 |
| 1.16.3.1 | malfunction |
deletion of the rv0846c gene increases the susceptibility of Mycobacterium tuberculosis to copper at least 10fold |
-, 763203 |
| 1.16.3.1 | malfunction |
knockdown of MCO1 is correlated with increased longevity on high-iron food and decreased iron accumulation |
728678 |
| 1.16.3.1 | malfunction |
strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin ferroxidase activity. The deficiency of ceruloplasmin ferroxidase activity in Ag-fed rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apolactoferrin (apo-LF) is administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron are restored more rapidly than in the control animals. Saturation of apo-LF with iron, provided by active ceruloplasmin, can strongly affect its protective capacity. Phenotype, overview |
-, 744470 |
| 1.16.3.1 | metabolism |
the initial step in the iron store mechanism occurs when the Fe(II) is oxidize to Fe(III) at the ferroxidase center (FC) found in the H-chain from mammalian ferritins, bacterial ferritins and Bfr subunits |
-, 746386 |
| 1.16.3.1 | more |
core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum. Fet3 protein lacking any one of the glycan units is found in an intracellular high-molecular mass species. But the missing carbohydrate is not required for native structure and biologic activity |
716849 |
| 1.16.3.1 | more |
Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview |
746541 |
