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Literature summary extracted from
- Investigation of the pH-dependent impact of sulfonated polyaniline on bioelectrocatalytic activity of xanthine dehydrogenase (2016), ACS Catal., 6, 7152-7159 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.17.1.4 | recombinant expression of His-tagged enzyme in Escherichia coli strain TP1000 | Rhodobacter capsulatus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | additional information | pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Macroporous ITO electrodes are used as an immobilization platform for the fabrication of HX-sensitive electrodes. The efficient polymer/enzyme interaction can be advantageously combined with the open structure of an electrode material of controlled pore size, resulting in good processability, stability, and defined signal transfer in the presence of a substrate. Method development and evaluation, overview | Rhodobacter capsulatus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.4 | hypoxanthine + NAD+ + 2 H2O | Rhodobacter capsulatus | - |
urate + NADH + H+ | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.1.4 | Rhodobacter capsulatus | O54050 AND O54051 | small and large subunits encoded by genes xdhA and xdhB | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.17.1.4 | recombinant His-tagged enzyme from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by gel filtration | Rhodobacter capsulatus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.4 | hypoxanthine + NAD+ + 2 H2O | - |
Rhodobacter capsulatus | urate + NADH + H+ | - |
? | |
| 1.17.1.4 | additional information | pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Method development and evaluation, overview | Rhodobacter capsulatus | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | XDH | - |
Rhodobacter capsulatus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.4 | 25 | - |
assay at | Rhodobacter capsulatus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.4 | 8 | - |
- |
Rhodobacter capsulatus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.4 | 4.5 | 9 | the enzyme is highly active at pH 5.0-8.0, shows low activity at pH 9.0, and is inactive above | Rhodobacter capsulatus |
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