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Literature summary for 1.1.99.29 extracted from
- Pyranose dehydrogenases Rare enzymes for electrochemistry and biocatalysis (2020), Bioelectrochemistry, 132, 107399 .
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars | Chlorophyllum rhacodes |
| analysis | pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars | Leucoagaricus meleagris |
| analysis | pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars | Agaricus bisporus |
| analysis | pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars | Agaricus xanthodermus |
| analysis | pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars | Agaricus campestris |
| biofuel production | pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures | Chlorophyllum rhacodes |
| biofuel production | pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures | Leucoagaricus meleagris |
| biofuel production | pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures | Agaricus bisporus |
| biofuel production | pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures | Agaricus xanthodermus |
| biofuel production | pyranose dehydrogenase is a promising candidate for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures | Agaricus campestris |
| synthesis | pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals | Chlorophyllum rhacodes |
| synthesis | pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals | Leucoagaricus meleagris |
| synthesis | pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals | Agaricus bisporus |
| synthesis | pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals | Agaricus xanthodermus |
| synthesis | pyranose dehydrogenase is a promising candidate for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals | Agaricus campestris |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Agaricus bisporus | Q3L1D1 | - |
- |
| Agaricus campestris | V5NDL4 | - |
- |
| Agaricus xanthodermus | V5NC32 | - |
- |
| Chlorophyllum rhacodes | - |
- |
- |
| Leucoagaricus meleagris | Q0R4L2 | - |
- |
| Leucoagaricus meleagris | Q3L243 | - |
- |
| Leucoagaricus meleagris | Q3L245 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | secretory glycosylated | Chlorophyllum rhacodes |
| glycoprotein | secretory glycosylated | Leucoagaricus meleagris |
| glycoprotein | secretory glycosylated | Agaricus bisporus |
| glycoprotein | secretory glycosylated | Agaricus xanthodermus |
| glycoprotein | secretory glycosylated | Agaricus campestris |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Chlorophyllum rhacodes |
| monomer | - |
Leucoagaricus meleagris |
| monomer | - |
Agaricus bisporus |
| monomer | - |
Agaricus xanthodermus |
| monomer | - |
Agaricus campestris |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDH | - |
Chlorophyllum rhacodes |
| PDH | - |
Leucoagaricus meleagris |
| PDH | - |
Agaricus bisporus |
| PDH | - |
Agaricus xanthodermus |
| PDH | - |
Agaricus campestris |
| pyranose dehydrogenase 1 | - |
Leucoagaricus meleagris |
| pyranose dehydrogenase 2 | - |
Leucoagaricus meleagris |
| pyranose dehydrogenase 3 | - |
Leucoagaricus meleagris |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | flavoprotein | Chlorophyllum rhacodes |  |
| FAD | flavoprotein | Leucoagaricus meleagris | |
| FAD | flavoprotein | Agaricus bisporus | |
| FAD | flavoprotein | Agaricus xanthodermus | |
| FAD | flavoprotein | Agaricus campestris | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Agaricus bisporus | generally low and probably constitutive transcription level and a moderate increase in transcription rate upon carbon depletion | up |
| Leucoagaricus meleagris | generally low and probably constitutive transcription level and a moderate increase in transcription rate upon carbon depletion. pdh1 shows a significantly higher transcription rate compared to pdh2 and pdh3, and stress-related induction upon oxygen deprivation | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | production of PDH is limited to the family of Agaricaceae | Chlorophyllum rhacodes |
| evolution | production of PDH is limited to the family of Agaricaceae | Leucoagaricus meleagris |
| evolution | production of PDH is limited to the family of Agaricaceae | Agaricus bisporus |
| evolution | production of PDH is limited to the family of Agaricaceae | Agaricus xanthodermus |
| evolution | production of PDH is limited to the family of Agaricaceae | Agaricus campestris |
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Release 2023.1 (January 2023)
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