EC Number   |
General Information |
Reference |
|---|
   1.8.3.2 | drug target |
QSOX is a potential target for blocking parasite transmission |
-, 764721 |
| 1.8.3.2 | evolution |
augmenter of liver regeneration is a member of the ERV family of small flavin-dependent sulfhydryl oxidases that contain a redox-active CxxC disulfide bond in redox communication with the isoalloxazine ring of bound FAD |
741890 |
| 1.8.3.2 | evolution |
based on the analysis of 33 fungal genomes, sulfhydryl oxidase (SOX) encoding genes are close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, the enzyme (AtSOX) is evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin (GliT, HlmI and DepH) are evolutionary closely related to AtSOX whereas fungal thioreductases are more distant |
-, 764376 |
| 1.8.3.2 | evolution |
enzyme QSOX is an evolutionarily conserved protein present in organisms ranging from the smallest free-living eukaryotes to humans |
741563 |
| 1.8.3.2 | evolution |
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa |
-, 742196 |
| 1.8.3.2 | evolution |
mechanistic parallels between the eukaryotic QSOX enzymes and the DsbA/B system catalyzing disulfide bond generation in the bacterial periplasm are detected suggesting that the strategy of linked disulfide exchanges may be exploited in other catalysts of oxidative protein folding |
742867 |
| 1.8.3.2 | evolution |
the enzyme belongs to a family of flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidases |
743627 |
| 1.8.3.2 | malfunction |
mutations at a cis-proline in QSOX1 that is conserved across the thioredoxin superfamily result in QSOX1 variants that showed a striking detrimental effect when added exogenously to fibroblasts. They severely disrupt the extracellular matrix and cell adhesion, even in the presence of naturally secreted, wild-type enzyme (QSOX1) |
765727 |
| 1.8.3.2 | malfunction |
Pbqsox deletion (DELTApbqsox) does not affect asexual intraerythrocytic development, but reduces exflagellation of male gametocytes as well as formation and maturation of ookinetes. Pbqsox deletion also leads to a significant increase in the reduced thiol groups of ookinete surface proteins |
-, 764721 |
| 1.8.3.2 | malfunction |
silencing Sfp53 expression does not rescue the ability of an ac92-knockout virus to produce infectious virus. Similarly, ac92 expression does not affect SfP53-stimulated caspase activity or the localization of SfP53. Although Ac92 binds to SfP53 during AcMNPV replication and oxidizes SfP53 in vitro, no effects of this interaction on AcMNPV replication in cultured cells can be detected. Overexpression or silencing of Ac92 during virus infection does not affect SfP53 accumulation |
743883 |
