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Literature summary extracted from
- The possible role of dermatophyte cysteine dioxygenase in keratin degradation (2013), Med. Mycol., 51, 449-454.
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.20 | L-cysteine + O2 | Mammalia | - |
3-sulfinoalanine | - |
? |  |
| 1.13.11.20 | L-cysteine + O2 | Bacillus sp. (in: Bacteria) | - |
3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | Candida albicans | - |
3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | Streptomyces sp. | - |
3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | Trichophyton rubrum | - |
3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | Histoplasma capsulatum | - |
3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | Trichophyton mentagrophytes | - |
3-sulfinoalanine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.20 | Bacillus sp. (in: Bacteria) | - |
- |
- |
| 1.13.11.20 | Candida albicans | - |
- |
- |
| 1.13.11.20 | Histoplasma capsulatum | - |
- |
- |
| 1.13.11.20 | Mammalia | - |
- |
- |
| 1.13.11.20 | Streptomyces sp. | - |
- |
- |
| 1.13.11.20 | Trichophyton mentagrophytes | - |
- |
- |
| 1.13.11.20 | Trichophyton rubrum | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.13.11.20 | keratinocyte | - |
Mammalia | - |
| 1.13.11.20 | additional information | in Bacillus and Streptomyces spp. CDO is expressed in the vegetative state, and an increase in its activity is detected after the initiation of conidia production | Bacillus sp. (in: Bacteria) | - |
| 1.13.11.20 | mycelium | in Streptomyces spp. CDO is expressed in the vegetative state, and an increase in its activity is detected after the initiation of conidia production | Streptomyces sp. | - |
| 1.13.11.20 | skin | - |
Mammalia | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.20 | L-cysteine + O2 | - |
Mammalia | 3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | - |
Bacillus sp. (in: Bacteria) | 3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | - |
Candida albicans | 3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | - |
Streptomyces sp. | 3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | - |
Trichophyton rubrum | 3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | - |
Histoplasma capsulatum | 3-sulfinoalanine | - |
? | |
| 1.13.11.20 | L-cysteine + O2 | - |
Trichophyton mentagrophytes | 3-sulfinoalanine | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.20 | CDO | - |
Mammalia |
| 1.13.11.20 | CDO | - |
Bacillus sp. (in: Bacteria) |
| 1.13.11.20 | CDO | - |
Candida albicans |
| 1.13.11.20 | CDO | - |
Streptomyces sp. |
| 1.13.11.20 | CDO | - |
Trichophyton rubrum |
| 1.13.11.20 | CDO | - |
Histoplasma capsulatum |
| 1.13.11.20 | CDO | - |
Trichophyton mentagrophytes |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.20 | metabolism | in mammals, excess cysteine is generally degraded by oxygenation to 3-sulfino-L-alanine. The majority of cysteine sulphinic acid is then deaminated to sulphinylpyruvate, which decomposes spontaneously byreleasing inorganic sulphite. The latter compound is then further oxidized to sulphate, which is excreted for the most part from the cell. In parallel, a variable proportion of cysteine sulphinic acid is decarboxylated to hypotaurine, then further oxidized to taurine. Although cysteine can be catabolized by some non-oxidative pathways, they are of minor importance. CDO activity is regulated by concentration of cysteine, and in mammals, both have been demonstrated to be important vital factors | Mammalia |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels, supplementation of growth medium with L-cystine induces a persistent increase in the CDO mRNA transcript level, whereas the concentration of intracellular CDO protein changes over time. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Trichophyton mentagrophytes |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Mammalia |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Bacillus sp. (in: Bacteria) |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Candida albicans |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Streptomyces sp. |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Trichophyton rubrum |
| 1.13.11.20 | additional information | intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. Mechanism of cysteine oxygenation from iron(II)-superoxo complex, via cis- and trans-sulfoxide structure formation, to iron(IV)-oxo complex and the final product cysteine sulphinic acid | Histoplasma capsulatum |
| 1.13.11.20 | physiological function | CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion | Bacillus sp. (in: Bacteria) |
| 1.13.11.20 | physiological function | CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion | Streptomyces sp. |
| 1.13.11.20 | physiological function | CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion. In dermatophytes, CDO is a virulence factor crucial for keratin degradation, role of cysteine dioxygenase in the degradation of keratinized tissues by dermatophytes, overview | Trichophyton rubrum |
| 1.13.11.20 | physiological function | CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion. In dermatophytes, CDO is a virulence factor crucial for keratin degradation, role of cysteine dioxygenase in the degradation of keratinized tissues by dermatophytes, overview | Trichophyton mentagrophytes |
| 1.13.11.20 | physiological function | CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion. In dermatophytes, CDO is a virulence factor crucial for keratin degradation, role of cysteine dioxygenase in the degradation of keratinized tissues by dermatophytes, overview. In Candida albicans upregulated expression of CDO is detected in the switch from white to opaque phenotypes [18]. In the latter, a reversible transition has been described between smooth white, dome-shaped yeast colonies (white) to circular or irregular-shaped colonies, composed of a mixture of yeast and fi lamentous cells (opaque) | Candida albicans |
| 1.13.11.20 | physiological function | cysteine dioxygenase is a key enzyme involved in the homeostatic regulation of cysteine level and in production of important oxidized metabolites of cysteine such as pyruvate, sulphite, sulphate, hypotaurine, and taurine in all eukaryotic cells, CDO is crucial for oxidation of cysteine to cysteine sulphinic acid and therefore for sulphite production and secretion | Mammalia |
| 1.13.11.20 | physiological function | in Histoplasma capsulatum, the enzyme is a key factor in the transition from the mycelial to yeast phase. CDO is crucial for oxidation of cysteine to cysteine sulfinic acid and therefore for sulfite production and secretion | Histoplasma capsulatum |
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