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Literature summary for 3.6.1.6 extracted from
- Changes in GDPase/UDPase enzymatic activity in response to oxidative stress in four Candida species (2015), Folia Microbiol. (Praha), 60, 343-350 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| H2O2 | in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2 | Candida albicans |  |
| H2O2 | in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2 | [Candida] glabrata | |
| H2O2 | in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2 | Candida parapsilosis | |
| H2O2 | in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2 | Pichia kudriavzevii | |
| menadione | - |
Candida albicans | |
| menadione | UDPase activity increases at lower concentrations of the oxidant and decreases at higher concentrations | [Candida] glabrata | |
| menadione | UDPase activity increases at lower concentrations of the oxidant and decreases at higher concentrations | Candida parapsilosis | |
| menadione | - |
Pichia kudriavzevii | |
| additional information | GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione | Candida albicans | |
| additional information | GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione | [Candida] glabrata | |
| additional information | GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione | Candida parapsilosis | |
| additional information | GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione | Pichia kudriavzevii | |
| superoxide | GDPase activity significantly decreases at high concentrations | Candida albicans | |
| superoxide | GDPase activity significantly decreases at high concentrations | [Candida] glabrata | |
| superoxide | GDPase activity significantly decreases at high concentrations | Candida parapsilosis | |
| superoxide | GDPase activity significantly decreases at high concentrations | Pichia kudriavzevii | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Pichia kudriavzevii | - |
- |
| microsome | - |
Candida albicans | - |
- |
| microsome | - |
Candida parapsilosis | - |
- |
| microsome | - |
[Candida] glabrata | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Pichia kudriavzevii | |
| Ca2+ | required | Candida albicans | |
| Ca2+ | required | Candida parapsilosis | |
| Ca2+ | required | [Candida] glabrata | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GDP + H2O | Pichia kudriavzevii | - |
GMP + phosphate | - |
? | |
| GDP + H2O | Candida albicans | - |
GMP + phosphate | - |
? | |
| GDP + H2O | Candida parapsilosis | - |
GMP + phosphate | - |
? | |
| GDP + H2O | [Candida] glabrata | - |
GMP + phosphate | - |
? | |
| UDP + H2O | Pichia kudriavzevii | - |
UMP + phosphate | - |
? | |
| UDP + H2O | Candida albicans | - |
UMP + phosphate | - |
? | |
| UDP + H2O | Candida parapsilosis | - |
UMP + phosphate | - |
? | |
| UDP + H2O | [Candida] glabrata | - |
UMP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Candida albicans | - |
clinical isolate from Mexico | - |
| Candida parapsilosis | - |
clinical isolate from Mexico | - |
| Pichia kudriavzevii | - |
clinical isolate from Mexico | - |
| [Candida] glabrata | - |
clinical isolate from Mexico | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GDP + H2O | - |
Pichia kudriavzevii | GMP + phosphate | - |
? | |
| GDP + H2O | - |
Candida albicans | GMP + phosphate | - |
? | |
| GDP + H2O | - |
Candida parapsilosis | GMP + phosphate | - |
? | |
| GDP + H2O | - |
[Candida] glabrata | GMP + phosphate | - |
? | |
| UDP + H2O | - |
Pichia kudriavzevii | UMP + phosphate | - |
? | |
| UDP + H2O | - |
Candida albicans | UMP + phosphate | - |
? | |
| UDP + H2O | - |
Candida parapsilosis | UMP + phosphate | - |
? | |
| UDP + H2O | - |
[Candida] glabrata | UMP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GDPase | - |
Pichia kudriavzevii |
| GDPase | - |
Candida albicans |
| GDPase | - |
Candida parapsilosis |
| GDPase | - |
[Candida] glabrata |
| GDPase/UDPase | - |
Pichia kudriavzevii |
| GDPase/UDPase | - |
Candida albicans |
| GDPase/UDPase | - |
Candida parapsilosis |
| GDPase/UDPase | - |
[Candida] glabrata |
| NDPase | - |
Pichia kudriavzevii |
| NDPase | - |
Candida albicans |
| NDPase | - |
Candida parapsilosis |
| NDPase | - |
[Candida] glabrata |
| UDPase | - |
Pichia kudriavzevii |
| UDPase | - |
Candida albicans |
| UDPase | - |
Candida parapsilosis |
| UDPase | - |
[Candida] glabrata |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Pichia kudriavzevii |
| 37 | - |
assay at | Candida albicans |
| 37 | - |
assay at | Candida parapsilosis |
| 37 | - |
assay at | [Candida] glabrata |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Pichia kudriavzevii |
| 7.5 | - |
assay at | Candida albicans |
| 7.5 | - |
assay at | Candida parapsilosis |
| 7.5 | - |
assay at | [Candida] glabrata |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview | Pichia kudriavzevii |
| metabolism | the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview | Candida albicans |
| metabolism | the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview | Candida parapsilosis |
| metabolism | the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview | [Candida] glabrata |
| physiological function | the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties | Pichia kudriavzevii |
| physiological function | the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties | Candida albicans |
| physiological function | the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties | Candida parapsilosis |
| physiological function | the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties | [Candida] glabrata |
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