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Literature summary for 1.17.1.4 extracted from
- Xanthine dehydrogenase an old enzyme with new knowledge and prospects (2016), Bioengineered, 7, 395-405 .
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | the enzyme can be useful in biotechnlogical applications requiring special conditions, e.g. extreme pH values | Acinetobacter baumannii |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Gallus gallus |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Drosophila melanogaster |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Homo sapiens |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Rattus norvegicus |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Bos taurus |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Ovis aries |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Enterobacter cloacae |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Pseudomonas putida |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Rhodobacter capsulatus |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Clostridium cylindrosporum |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Micrococcus sp. |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Acinetobacter baumannii |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Streptomyces cyanogenus |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Arabidopsis thaliana |
| environmental protection | XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin | Arthrobacter luteolus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene xdh, sequence comparisons and phylogenetic analysis | Gallus gallus |
| gene xdh, sequence comparisons and phylogenetic analysis | Drosophila melanogaster |
| gene xdh, sequence comparisons and phylogenetic analysis | Homo sapiens |
| gene xdh, sequence comparisons and phylogenetic analysis | Bos taurus |
| gene xdh, sequence comparisons and phylogenetic analysis | Ovis aries |
| gene xdh, sequence comparisons and phylogenetic analysis | Enterobacter cloacae |
| gene xdh, sequence comparisons and phylogenetic analysis | Pseudomonas putida |
| gene xdh, sequence comparisons and phylogenetic analysis | Clostridium cylindrosporum |
| gene xdh, sequence comparisons and phylogenetic analysis | Micrococcus sp. |
| gene xdh, sequence comparisons and phylogenetic analysis | Streptomyces cyanogenus |
| gene xdh, sequence comparisons and phylogenetic analysis | Arthrobacter luteolus |
| gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli | Rhodobacter capsulatus |
| gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli | Acinetobacter baumannii |
| gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli | Escherichia coli |
| gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris | Arabidopsis thaliana |
| gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression of liver XDH in insect cell system | Rattus norvegicus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure determination | Homo sapiens |
| crystal structure determination | Rattus norvegicus |
| crystal structure determination | Bos taurus |
| crystal structure determination | Rhodobacter capsulatus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Bos taurus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | in the [2Fe-2S] center | Gallus gallus |  |
| Fe2+ | in the [2Fe-2S] center | Drosophila melanogaster | |
| Fe2+ | in the [2Fe-2S] center | Homo sapiens | |
| Fe2+ | in the [2Fe-2S] center | Rattus norvegicus | |
| Fe2+ | in the [2Fe-2S] center | Bos taurus | |
| Fe2+ | in the [2Fe-2S] center | Ovis aries | |
| Fe2+ | in the [2Fe-2S] center | Enterobacter cloacae | |
| Fe2+ | in the [2Fe-2S] center | Pseudomonas putida | |
| Fe2+ | in the [2Fe-2S] center | Rhodobacter capsulatus | |
| Fe2+ | in the [2Fe-2S] center | Clostridium cylindrosporum | |
| Fe2+ | in the [2Fe-2S] center | Micrococcus sp. | |
| Fe2+ | in the [2Fe-2S] center | Acinetobacter baumannii | |
| Fe2+ | in the [2Fe-2S] center | Streptomyces cyanogenus | |
| Fe2+ | in the [2Fe-2S] center | Arabidopsis thaliana | |
| Fe2+ | in the [2Fe-2S] center | Escherichia coli | |
| Fe2+ | in the [2Fe-2S] center | Acinetobacter phage Ab105-3phi | |
| Fe2+ | in the [2Fe-2S] center | Arthrobacter luteolus | |
| Molybdenum | a molybdenum-containing flavoprotein | Gallus gallus | |
| Molybdenum | a molybdenum-containing flavoprotein | Drosophila melanogaster | |
| Molybdenum | a molybdenum-containing flavoprotein | Homo sapiens | |
| Molybdenum | a molybdenum-containing flavoprotein | Rattus norvegicus | |
| Molybdenum | a molybdenum-containing flavoprotein | Bos taurus | |
| Molybdenum | a molybdenum-containing flavoprotein | Ovis aries | |
| Molybdenum | a molybdenum-containing flavoprotein | Enterobacter cloacae | |
| Molybdenum | a molybdenum-containing flavoprotein | Pseudomonas putida | |
| Molybdenum | a molybdenum-containing flavoprotein | Rhodobacter capsulatus | |
| Molybdenum | a molybdenum-containing flavoprotein | Clostridium cylindrosporum | |
| Molybdenum | a molybdenum-containing flavoprotein | Micrococcus sp. | |
| Molybdenum | a molybdenum-containing flavoprotein | Acinetobacter baumannii | |
| Molybdenum | a molybdenum-containing flavoprotein | Streptomyces cyanogenus | |
| Molybdenum | a molybdenum-containing flavoprotein | Escherichia coli | |
| Molybdenum | a molybdenum-containing flavoprotein | Acinetobacter phage Ab105-3phi | |
| Molybdenum | a molybdenum-containing flavoprotein | Arthrobacter luteolus | |
| Molybdenum | a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview | Arabidopsis thaliana | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 128000 | - |
- |
Enterobacter cloacae |
| 160000 | - |
- |
Escherichia coli |
| 160000 | - |
- |
Arthrobacter luteolus |
| 270000 | - |
- |
Rhodobacter capsulatus |
| 290000 | - |
- |
Bos taurus |
| 290000 | - |
- |
Acinetobacter baumannii |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| xanthine + NAD+ + H2O | Gallus gallus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Drosophila melanogaster | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Homo sapiens | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Rattus norvegicus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Bos taurus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Ovis aries | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Enterobacter cloacae | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Pseudomonas putida | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Rhodobacter capsulatus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Clostridium cylindrosporum | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Micrococcus sp. | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Acinetobacter baumannii | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Streptomyces cyanogenus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Arabidopsis thaliana | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Escherichia coli | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Acinetobacter phage Ab105-3phi | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Arthrobacter luteolus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Rhodobacter capsulatus B10XDHB | - |
urate + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acinetobacter baumannii | - |
- |
- |
| Acinetobacter phage Ab105-3phi | - |
- |
- |
| Arabidopsis thaliana | Q8GUQ8 | - |
- |
| Arthrobacter luteolus | - |
- |
- |
| Bos taurus | - |
- |
- |
| Clostridium cylindrosporum | - |
- |
- |
| Drosophila melanogaster | - |
- |
- |
| Enterobacter cloacae | - |
- |
- |
| Escherichia coli | Q46799 AND Q46800 | subunits encoding genes xdhA and xdhB | - |
| Gallus gallus | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Micrococcus sp. | - |
- |
- |
| Ovis aries | - |
- |
- |
| Pseudomonas putida | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Rhodobacter capsulatus | - |
- |
- |
| Rhodobacter capsulatus B10XDHB | - |
- |
- |
| Streptomyces cyanogenus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme | Enterobacter cloacae |
| purification of native enzyme | Arthrobacter luteolus |
| purification of native XDH | Gallus gallus |
| purification of native XDH | Drosophila melanogaster |
| purification of native XDH | Homo sapiens |
| purification of native XDH | Rattus norvegicus |
| purification of native XDH | Ovis aries |
| purification of native XDH | Rhodobacter capsulatus |
| purification of native XDH | Clostridium cylindrosporum |
| purification of native XDH | Micrococcus sp. |
| purification of native XDH | Streptomyces cyanogenus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
| milk | - |
Bos taurus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.8 | - |
purified native enzyme, pH and temperature not specified in the publication | Bos taurus |
| 7 | - |
purified recombinant enzyme, pH and temperature not specified in the publication | Escherichia coli |
| 7.5 | - |
purified native enzyme, pH and temperature not specified in the publication | Enterobacter cloacae |
| 10 | - |
purified native enzyme, pH and temperature not specified in the publication | Arthrobacter luteolus |
| 17.5 | - |
purified enzyme, pH and temperature not specified in the publication | Rhodobacter capsulatus |
| 29.1 | - |
purified recombinant enzyme, pH and temperature not specified in the publication | Acinetobacter baumannii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Gallus gallus | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Drosophila melanogaster | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Homo sapiens | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Rattus norvegicus | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Bos taurus | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Ovis aries | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Enterobacter cloacae | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Pseudomonas putida | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Rhodobacter capsulatus | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Clostridium cylindrosporum | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Micrococcus sp. | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Acinetobacter baumannii | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Streptomyces cyanogenus | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Arabidopsis thaliana | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Escherichia coli | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Acinetobacter phage Ab105-3phi | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Arthrobacter luteolus | ? | - |
? | |
| additional information | The enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD+ or NADP+ as electron acceptor, and in some species can be transformed to xanthine oxidase (EC 1.17.3.2, XOD) capable of utilizing oxygen as the electron acceptor | Rhodobacter capsulatus B10XDHB | ? | - |
? | |
| xanthine + NAD+ + H2O | - |
Gallus gallus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Drosophila melanogaster | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Homo sapiens | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Rattus norvegicus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Bos taurus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Ovis aries | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Enterobacter cloacae | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Pseudomonas putida | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Rhodobacter capsulatus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Clostridium cylindrosporum | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Micrococcus sp. | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Acinetobacter baumannii | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Streptomyces cyanogenus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Arabidopsis thaliana | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Escherichia coli | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Acinetobacter phage Ab105-3phi | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Arthrobacter luteolus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Rhodobacter capsulatus B10XDHB | urate + NADH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 69000 | Enterobacter cloacae |
| homodimer | 2 * 145000, the enzyme exists as (alpha)2 form | Bos taurus |
| homodimer | 2 * 80000, (alpha)2 | Arthrobacter luteolus |
| homodimer | the enzyme exists as (alpha)2 form | Gallus gallus |
| homodimer | the enzyme exists as (alpha)2 form | Rattus norvegicus |
| homodimer | the enzyme exists as (alpha)2 form | Arabidopsis thaliana |
| More | bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4 and alphabetagamma forms | Rhodobacter capsulatus |
| More | bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4, and alphabetagamma forms | Pseudomonas putida |
| More | bacterial XDHs, including Rhodobacter capsulatus, Pseudomonas putida and Streptomyces cyanogenus, are found in the alpha2, alpha4, (alphabeta)2, (alphabeta)4, and alphabetagamma forms | Streptomyces cyanogenus |
| tetramer | 2 * 50000, alpha-subunit, + 2 * 80000, beta-subunit, alpha2beta2 | Rhodobacter capsulatus |
| tetramer | 2 * 87000, alpha-subunit, + 2 * 56000, beta-subunit, alpha2beta2 | Acinetobacter baumannii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| XDH | - |
Gallus gallus |
| XDH | - |
Drosophila melanogaster |
| XDH | - |
Homo sapiens |
| XDH | - |
Rattus norvegicus |
| XDH | - |
Bos taurus |
| XDH | - |
Ovis aries |
| XDH | - |
Enterobacter cloacae |
| XDH | - |
Pseudomonas putida |
| XDH | - |
Rhodobacter capsulatus |
| XDH | - |
Clostridium cylindrosporum |
| XDH | - |
Micrococcus sp. |
| XDH | - |
Acinetobacter baumannii |
| XDH | - |
Streptomyces cyanogenus |
| XDH | - |
Arabidopsis thaliana |
| XDH | - |
Escherichia coli |
| XDH | - |
Acinetobacter phage Ab105-3phi |
| XDH | - |
Arthrobacter luteolus |
| XDH1 | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 35 | - |
Bos taurus |
| 35 | 40 | - |
Rhodobacter capsulatus |
| 35 | 45 | - |
Enterobacter cloacae |
| 55 | 60 | - |
Arthrobacter luteolus |
| 65 | - |
- |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 25 | - |
xanthine | pH and temperature not specified in the publication | Acinetobacter baumannii | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7.5 | - |
Enterobacter cloacae |
| 7.5 | 8.5 | - |
Rhodobacter capsulatus |
| 7.5 | 8 | - |
Escherichia coli |
| 7.5 | 8 | - |
Arthrobacter luteolus |
| 8.5 | - |
- |
Bos taurus |
| 8.5 | 9 | - |
Acinetobacter baumannii |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
Acinetobacter baumannii XDH extends the pH tolerance to pH 11.0 | Acinetobacter baumannii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | a molybdenum-containing flavoprotein | Gallus gallus | |
| FAD | a molybdenum-containing flavoprotein | Drosophila melanogaster | |
| FAD | a molybdenum-containing flavoprotein | Homo sapiens | |
| FAD | a molybdenum-containing flavoprotein | Rattus norvegicus | |
| FAD | a molybdenum-containing flavoprotein | Bos taurus | |
| FAD | a molybdenum-containing flavoprotein | Ovis aries | |
| FAD | a molybdenum-containing flavoprotein | Enterobacter cloacae | |
| FAD | a molybdenum-containing flavoprotein | Pseudomonas putida | |
| FAD | a molybdenum-containing flavoprotein | Rhodobacter capsulatus | |
| FAD | a molybdenum-containing flavoprotein | Clostridium cylindrosporum | |
| FAD | a molybdenum-containing flavoprotein | Micrococcus sp. | |
| FAD | a molybdenum-containing flavoprotein | Acinetobacter baumannii | |
| FAD | a molybdenum-containing flavoprotein | Streptomyces cyanogenus | |
| FAD | a molybdenum-containing flavoprotein | Arabidopsis thaliana | |
| FAD | a molybdenum-containing flavoprotein | Escherichia coli | |
| FAD | a molybdenum-containing flavoprotein | Acinetobacter phage Ab105-3phi | |
| FAD | a molybdenum-containing flavoprotein | Arthrobacter luteolus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Gallus gallus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Drosophila melanogaster | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Homo sapiens | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Rattus norvegicus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Bos taurus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Ovis aries | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Enterobacter cloacae | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Pseudomonas putida | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Rhodobacter capsulatus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Clostridium cylindrosporum | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Micrococcus sp. | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Acinetobacter baumannii | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Streptomyces cyanogenus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Arabidopsis thaliana | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Acinetobacter phage Ab105-3phi | |
| molybdenum cofactor | a molybdenum-containing flavoprotein | Arthrobacter luteolus | |
| molybdenum cofactor | a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview | Escherichia coli | |
| additional information | cofactor domain amino acid sequence comparisons, overview | Acinetobacter phage Ab105-3phi | |
| additional information | cofactor domain amino acid sequence comparisons, overview | Arthrobacter luteolus | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Enterobacter cloacae | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Gallus gallus | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Drosophila melanogaster | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Homo sapiens | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Rattus norvegicus | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Bos taurus | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Ovis aries | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Pseudomonas putida | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Clostridium cylindrosporum | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Micrococcus sp. | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Acinetobacter baumannii | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Streptomyces cyanogenus | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Arabidopsis thaliana | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species | Escherichia coli | |
| additional information | cofactor domain amino acid sequence comparisons, overview. XDH consists of 3 redox center domains, XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]), another that includes a flavin adenine dinucleotide (FAD), and a third that incorporates a sulfurated molybdenum cofactor (Moco). The [2Fe-2S] domain is more conserved than the Moco domain, and the FAD domain is the least conserved one between different species. Rhodobacter capsulatus alpha2beta2 XDH arranges the FAD and [2Fe-2S] domains and the Moco domain into 2 separate subunits | Rhodobacter capsulatus | |
| NAD+ | - |
Gallus gallus | |
| NAD+ | - |
Drosophila melanogaster | |
| NAD+ | - |
Homo sapiens | |
| NAD+ | - |
Rattus norvegicus | |
| NAD+ | - |
Bos taurus | |
| NAD+ | - |
Ovis aries | |
| NAD+ | - |
Enterobacter cloacae | |
| NAD+ | - |
Pseudomonas putida | |
| NAD+ | - |
Rhodobacter capsulatus | |
| NAD+ | - |
Clostridium cylindrosporum | |
| NAD+ | - |
Micrococcus sp. | |
| NAD+ | - |
Acinetobacter baumannii | |
| NAD+ | - |
Streptomyces cyanogenus | |
| NAD+ | - |
Arabidopsis thaliana | |
| NAD+ | - |
Escherichia coli | |
| NAD+ | - |
Acinetobacter phage Ab105-3phi | |
| NAD+ | - |
Arthrobacter luteolus | |
| [2Fe-2S]-center | - |
Acinetobacter phage Ab105-3phi | |
| [2Fe-2S]-center | - |
Arthrobacter luteolus | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Gallus gallus | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Drosophila melanogaster | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Homo sapiens | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Rattus norvegicus | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Bos taurus | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Ovis aries | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Enterobacter cloacae | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Pseudomonas putida | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Rhodobacter capsulatus | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Clostridium cylindrosporum | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Micrococcus sp. | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Acinetobacter baumannii | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Streptomyces cyanogenus | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Arabidopsis thaliana | |
| [2Fe-2S]-center | XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S]) | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Gallus gallus |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Drosophila melanogaster |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Homo sapiens |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Rattus norvegicus |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Bos taurus |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Ovis aries |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Enterobacter cloacae |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Pseudomonas putida |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Rhodobacter capsulatus |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Clostridium cylindrosporum |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Micrococcus sp. |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Streptomyces cyanogenus |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Arabidopsis thaliana |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Escherichia coli |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis | Arthrobacter luteolus |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis. The page XDH sequence shows 100% identity to the genomic XDH genes of Acinetobacter baumannii. It seems plausible that the similarity is a result of horizontal gene transfer | Acinetobacter phage Ab105-3phi |
| evolution | XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis. The unique industrially applicable Acinetobacter baumannii XDH shows only modest similarity to all the previous already-characterized XDHs | Acinetobacter baumannii |
| additional information | Glu802 binds the substrate and stabilizes the transition state, Glu1261 is the catalytic base, Arg880 and Thr1010 bind the substrate and decrease the reaction activation energy, Phe914 and Phe1009 orientate the substrate via pi-pi stacking, Val1011 is the key residue channeling the substrate, and Gln758 is responsible for releasing the product. There is an obvious variation of key residues channeling the substrate and binding pocket, which affect the substrate entry and product release, resulting in different catalytic activity and enzymatic properties. Surprisingly, the 2 pairs of cysteines, C535 and C992, and C1316 and C1324 numbering in bovine XDH, which are proposed to control the reversible post-translational conversion from XDH to XOD, EC 1.17.3.2, by forming 2 cysteine disulfide bonds, are totally absent in other XDHs. Bovine milk XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview | Bos taurus |
| additional information | rat liver XDH can be converted reversibly into active XOD form by forming disulfide bond or irreversibly by limited proteolysis, overview | Rattus norvegicus |
| additional information | the Arabidopsis thaliana XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues | Arabidopsis thaliana |
| additional information | the chicken XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues | Gallus gallus |
| additional information | the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues | Rhodobacter capsulatus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Gallus gallus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Drosophila melanogaster |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Homo sapiens |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Rattus norvegicus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Bos taurus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Ovis aries |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Acinetobacter baumannii |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Arabidopsis thaliana |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Acinetobacter phage Ab105-3phi |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts | Arthrobacter luteolus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Enterobacter cloacae |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Pseudomonas putida |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Rhodobacter capsulatus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Clostridium cylindrosporum |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Micrococcus sp. |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Streptomyces cyanogenus |
| physiological function | XDHs play significant roles in various cellular processes, including purine catabolism and production of reactive oxygen species (ROS) and nitric oxide (NO) in both physiological and pathological contexts. Physiological roles and applications of bacterial XDHs, overview | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2740 | - |
xanthine | pH and temperature not specified in the publication | Acinetobacter baumannii | |
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