Inhibitors | Comment | Organism | Structure |
---|---|---|---|
zinc sulfate | 10 mM, completely inhibited | Aspergillus tubingensis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.8 | - |
glutathione | pH 7.4, 20°C | Aspergillus tubingensis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Aspergillus tubingensis | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
- |
Aspergillus tubingensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus tubingensis | - |
- |
- |
Aspergillus tubingensis D-85248 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Aspergillus tubingensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 D-cysteine + O2 | - |
Aspergillus tubingensis | D-cystine + H2O2 | - |
? | |
2 D-cysteine + O2 | - |
Aspergillus tubingensis D-85248 | D-cystine + H2O2 | - |
? | |
2 dithiothreitol + O2 | - |
Aspergillus tubingensis | dithiothreitol disulfide + H2O2 | - |
? | |
2 dithiothreitol + O2 | - |
Aspergillus tubingensis D-85248 | dithiothreitol disulfide + H2O2 | - |
? | |
2 glutathione + O2 | the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol | Aspergillus tubingensis | glutathione disulfide + H2O2 | - |
? | |
2 glutathione + O2 | the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol | Aspergillus tubingensis D-85248 | glutathione disulfide + H2O2 | - |
? | |
additional information | peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme | Aspergillus tubingensis | ? | - |
- |
|
additional information | peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme | Aspergillus tubingensis D-85248 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
AtSOX | - |
Aspergillus tubingensis |
sulfhydryl oxidase | - |
Aspergillus tubingensis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
the enzyme retains 89% of the initial activity after 20 h incubation | Aspergillus tubingensis |
50 | - |
the enzyme retains 75% of the initial activity after 20 h incubation | Aspergillus tubingensis |
60 | - |
the enzyme retains 18% of the initial activity after 20 h incubation | Aspergillus tubingensis |
70 | - |
the enzyme is inactivated within 15 min | Aspergillus tubingensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Aspergillus tubingensis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4 | 8.5 | retains more than 80% of the initial activity in a pH range 4-8.5 within 20 h | Aspergillus tubingensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the enzyme contains a non-covalently bound flavin cofactor | Aspergillus tubingensis |
General Information | Comment | Organism |
---|---|---|
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 | Aspergillus tubingensis |
physiological function | SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides | Aspergillus tubingensis |