BRENDA - Enzyme Database

Xanthine dehydrogenase an old enzyme with new knowledge and prospects

Wang, C.H.; Zhang, C.; Xing, X.H.; Bioengineered 7, 395-405 (2016)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
1.17.1.4
biotechnology
the enzyme can be useful in biotechnlogical applications requiring special conditions, e.g. extreme pH values
Acinetobacter baumannii
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Acinetobacter baumannii
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Arabidopsis thaliana
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Arthrobacter luteolus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Bos taurus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Clostridium cylindrosporum
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Drosophila melanogaster
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Enterobacter cloacae
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Gallus gallus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Homo sapiens
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Micrococcus sp.
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Ovis aries
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Pseudomonas putida
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Rattus norvegicus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Rhodobacter capsulatus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Streptomyces cyanogenus
Cloned(Commentary)
EC Number
Commentary
Organism
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Arthrobacter luteolus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Bos taurus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Clostridium cylindrosporum
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Drosophila melanogaster
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Enterobacter cloacae
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Gallus gallus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Homo sapiens
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Micrococcus sp.
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Ovis aries
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Pseudomonas putida
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Streptomyces cyanogenus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
Acinetobacter baumannii
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
Escherichia coli
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
Rhodobacter capsulatus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
Arabidopsis thaliana
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression of liver XDH in insect cell system
Rattus norvegicus
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.17.1.4
crystal structure determination
Bos taurus
1.17.1.4
crystal structure determination
Homo sapiens
1.17.1.4
crystal structure determination
Rattus norvegicus
1.17.1.4
crystal structure determination
Rhodobacter capsulatus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.17.1.4
extracellular
-
Bos taurus
-
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.17.1.4
Fe2+
in the [2Fe-2S] center
Acinetobacter baumannii
1.17.1.4
Fe2+
in the [2Fe-2S] center
Acinetobacter phage Ab105-3phi
1.17.1.4
Fe2+
in the [2Fe-2S] center
Arabidopsis thaliana
1.17.1.4
Fe2+
in the [2Fe-2S] center
Arthrobacter luteolus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Bos taurus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Clostridium cylindrosporum
1.17.1.4
Fe2+
in the [2Fe-2S] center
Drosophila melanogaster
1.17.1.4
Fe2+
in the [2Fe-2S] center
Enterobacter cloacae
1.17.1.4
Fe2+
in the [2Fe-2S] center
Escherichia coli
1.17.1.4
Fe2+
in the [2Fe-2S] center
Gallus gallus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Homo sapiens
1.17.1.4
Fe2+
in the [2Fe-2S] center
Micrococcus sp.
1.17.1.4
Fe2+
in the [2Fe-2S] center
Ovis aries
1.17.1.4
Fe2+
in the [2Fe-2S] center
Pseudomonas putida
1.17.1.4
Fe2+
in the [2Fe-2S] center
Rattus norvegicus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Rhodobacter capsulatus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Streptomyces cyanogenus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Acinetobacter baumannii
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Acinetobacter phage Ab105-3phi
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Arabidopsis thaliana
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Arthrobacter luteolus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Bos taurus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Clostridium cylindrosporum
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Drosophila melanogaster
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Enterobacter cloacae
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Escherichia coli
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Gallus gallus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Homo sapiens
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Micrococcus sp.
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Ovis aries
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Pseudomonas putida
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Rattus norvegicus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Rhodobacter capsulatus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Streptomyces cyanogenus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.17.1.4
128000
-
-
Enterobacter cloacae
1.17.1.4
160000
-
-
Arthrobacter luteolus
1.17.1.4
160000
-
-
Escherichia coli
1.17.1.4
270000
-
-
Rhodobacter capsulatus
1.17.1.4
290000
-
-
Acinetobacter baumannii
1.17.1.4
290000
-
-
Bos taurus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.17.1.4
xanthine + NAD+ + H2O
Gallus gallus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Drosophila melanogaster
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Homo sapiens
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Rattus norvegicus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Bos taurus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Ovis aries
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Enterobacter cloacae
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Pseudomonas putida
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Rhodobacter capsulatus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Clostridium cylindrosporum
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Micrococcus sp.
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Acinetobacter baumannii
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Streptomyces cyanogenus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Arabidopsis thaliana
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Escherichia coli
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Acinetobacter phage Ab105-3phi
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Arthrobacter luteolus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Rhodobacter capsulatus B10XDHB
-
urate + NADH + H+
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.17.1.4
Acinetobacter baumannii
-
-
-
1.17.1.4
Acinetobacter phage Ab105-3phi
-
-
-
1.17.1.4
Arabidopsis thaliana
Q8GUQ8
-
-
1.17.1.4
Arthrobacter luteolus
-
-
-
1.17.1.4
Bos taurus
-
-
-
1.17.1.4
Clostridium cylindrosporum
-
-
-
1.17.1.4
Drosophila melanogaster
-
-
-
1.17.1.4
Enterobacter cloacae
-
-
-
1.17.1.4
Escherichia coli
Q46799 AND Q46800
subunits encoding genes xdhA and xdhB
-
1.17.1.4
Gallus gallus
-
-
-
1.17.1.4
Homo sapiens
-
-
-
1.17.1.4
Micrococcus sp.
-
-
-
1.17.1.4
Ovis aries
-
-
-
1.17.1.4
Pseudomonas putida
-
-
-
1.17.1.4
Rattus norvegicus
-
-
-
1.17.1.4
Rhodobacter capsulatus
-
-
-
1.17.1.4
Rhodobacter capsulatus B10XDHB
-
-
-
1.17.1.4
Streptomyces cyanogenus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.17.1.4
native enzyme
Enterobacter cloacae
1.17.1.4
purification of native enzyme
Arthrobacter luteolus
1.17.1.4
purification of native XDH
Clostridium cylindrosporum
1.17.1.4
purification of native XDH
Drosophila melanogaster
1.17.1.4
purification of native XDH
Gallus gallus
1.17.1.4
purification of native XDH
Homo sapiens
1.17.1.4
purification of native XDH
Micrococcus sp.
1.17.1.4
purification of native XDH
Ovis aries
1.17.1.4
purification of native XDH
Rattus norvegicus
1.17.1.4
purification of native XDH
Rhodobacter capsulatus
1.17.1.4
purification of native XDH
Streptomyces cyanogenus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.17.1.4
liver
-
Rattus norvegicus
-
1.17.1.4
milk
-
Bos taurus
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
1.17.1.4
1.8
-
purified native enzyme, pH and temperature not specified in the publication
Bos taurus
1.17.1.4
7
-
purified recombinant enzyme, pH and temperature not specified in the publication
Escherichia coli
1.17.1.4
7.5
-
purified native enzyme, pH and temperature not specified in the publication
Enterobacter cloacae
1.17.1.4
10
-
purified native enzyme, pH and temperature not specified in the publication
Arthrobacter luteolus
1.17.1.4
17.5
-
purified enzyme, pH and temperature not specified in the publication
Rhodobacter capsulatus
1.17.1.4
29.1
-
purified recombinant enzyme, pH and temperature not specified in the publication
Acinetobacter baumannii
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.17.1.4
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
744450
Gallus gallus
?
-
-
-
-
1.17.1.4
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
744450
Drosophila melanogaster
?
-
-
-
-
1.17.1.4
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
744450
Homo sapiens
?
-
-
-
-
1.17.1.4
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
744450
Rattus norvegicus
?
-
-
-
-
1.17.1.4
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
744450
Bos taurus
?
-
-
-
-
1.17.1.4
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
744450
Ovis aries
?
-
-
-
-
1.17.1.4
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
744450
Enterobacter cloacae
?
-
-
-
-
1.17.1.4
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
744450
Pseudomonas putida
?
-
-
-
-
1.17.1.4
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
744450
Rhodobacter capsulatus
?
-
-
-
-
1.17.1.4
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
744450
Clostridium cylindrosporum
?
-
-
-
-
1.17.1.4
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
744450
Micrococcus sp.
?
-
-
-
-
1.17.1.4
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
744450
Acinetobacter baumannii
?
-
-
-
-
1.17.1.4
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
744450
Streptomyces cyanogenus
?
-
-
-
-
1.17.1.4
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
744450
Arabidopsis thaliana
?
-
-
-
-
1.17.1.4
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
744450
Escherichia coli
?
-
-
-
-
1.17.1.4
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
744450
Acinetobacter phage Ab105-3phi
?
-
-
-
-
1.17.1.4
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
744450
Arthrobacter luteolus
?
-
-
-
-
1.17.1.4
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
744450
Rhodobacter capsulatus B10XDHB
?
-
-
-
-
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Gallus gallus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Drosophila melanogaster
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Homo sapiens
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Rattus norvegicus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Bos taurus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Ovis aries
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Enterobacter cloacae
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Pseudomonas putida
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Rhodobacter capsulatus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Clostridium cylindrosporum
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Micrococcus sp.
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Acinetobacter baumannii
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Streptomyces cyanogenus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Arabidopsis thaliana
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Escherichia coli
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Acinetobacter phage Ab105-3phi
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Arthrobacter luteolus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Rhodobacter capsulatus B10XDHB
urate + NADH + H+
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.17.1.4
homodimer
the enzyme exists as (alpha)2 form
Arabidopsis thaliana
1.17.1.4
homodimer
2 * 80000, (alpha)2
Arthrobacter luteolus
1.17.1.4
homodimer
2 * 145000, the enzyme exists as (alpha)2 form
Bos taurus
1.17.1.4
homodimer
2 * 69000
Enterobacter cloacae
1.17.1.4
homodimer
the enzyme exists as (alpha)2 form
Gallus gallus
1.17.1.4
homodimer
the enzyme exists as (alpha)2 form
Rattus norvegicus
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
tetramer
2 * 87000, alpha-subunit, + 2 * 56000, beta-subunit, alpha2beta2
Acinetobacter baumannii
1.17.1.4
tetramer
2 * 50000, alpha-subunit, + 2 * 80000, beta-subunit, alpha2beta2
Rhodobacter capsulatus
Temperature Optimum [░C]
EC Number
Temperature Optimum [░C]
Temperature Optimum Maximum [░C]
Commentary
Organism
1.17.1.4
25
35
-
Bos taurus
1.17.1.4
35
40
-
Rhodobacter capsulatus
1.17.1.4
35
45
-
Enterobacter cloacae
1.17.1.4
55
60
-
Arthrobacter luteolus
1.17.1.4
65
-
-
Escherichia coli
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.17.1.4
25
-
xanthine
pH and temperature not specified in the publication
Acinetobacter baumannii
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.17.1.4
6.5
7.5
-
Enterobacter cloacae
1.17.1.4
7.5
8
-
Arthrobacter luteolus
1.17.1.4
7.5
8
-
Escherichia coli
1.17.1.4
7.5
8.5
-
Rhodobacter capsulatus
1.17.1.4
8.5
9
-
Acinetobacter baumannii
1.17.1.4
8.5
-
-
Bos taurus
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.17.1.4
additional information
-
Acinetobacter baumannii XDH extends the pH tolerance to pH 11.0
Acinetobacter baumannii
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Acinetobacter baumannii
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Acinetobacter phage Ab105-3phi
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Arabidopsis thaliana
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Arthrobacter luteolus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Bos taurus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Clostridium cylindrosporum
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Drosophila melanogaster
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Enterobacter cloacae
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Escherichia coli
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Gallus gallus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Homo sapiens
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Micrococcus sp.
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Ovis aries
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Pseudomonas putida
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Rattus norvegicus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Rhodobacter capsulatus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Streptomyces cyanogenus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Acinetobacter baumannii
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Acinetobacter phage Ab105-3phi
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Arabidopsis thaliana
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Arthrobacter luteolus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Bos taurus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Clostridium cylindrosporum
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Drosophila melanogaster
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Enterobacter cloacae
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Escherichia coli
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Gallus gallus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Homo sapiens
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Micrococcus sp.
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Ovis aries
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Pseudomonas putida
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Rattus norvegicus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Rhodobacter capsulatus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Streptomyces cyanogenus
1.17.1.4
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
1.17.1.4
additional information
cofactor domain amino acid sequence comparisons, overview
Acinetobacter phage Ab105-3phi
1.17.1.4
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
1.17.1.4
additional information
cofactor domain amino acid sequence comparisons, overview
Arthrobacter luteolus
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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.
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
NAD+
-
Acinetobacter baumannii
1.17.1.4
NAD+
-
Acinetobacter phage Ab105-3phi
1.17.1.4
NAD+
-
Arthrobacter luteolus
1.17.1.4
NAD+
-
Bos taurus
1.17.1.4
NAD+
-
Clostridium cylindrosporum
1.17.1.4
NAD+
-
Drosophila melanogaster
1.17.1.4
NAD+
-
Enterobacter cloacae
1.17.1.4
NAD+
-
Escherichia coli
1.17.1.4
NAD+
-
Gallus gallus
1.17.1.4
NAD+
-
Homo sapiens
1.17.1.4
NAD+
-
Micrococcus sp.
1.17.1.4
NAD+
-
Ovis aries
1.17.1.4
NAD+
-
Pseudomonas putida
1.17.1.4
NAD+
-
Streptomyces cyanogenus
1.17.1.4
NAD+
-
Rattus norvegicus
1.17.1.4
NAD+
-
Rhodobacter capsulatus
1.17.1.4
NAD+
-
Arabidopsis thaliana
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Acinetobacter baumannii
1.17.1.4
[2Fe-2S]-center
-
Acinetobacter phage Ab105-3phi
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Arabidopsis thaliana
1.17.1.4
[2Fe-2S]-center
-
Arthrobacter luteolus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Bos taurus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Clostridium cylindrosporum
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Drosophila melanogaster
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Enterobacter cloacae
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Escherichia coli
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Gallus gallus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Homo sapiens
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Micrococcus sp.
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Ovis aries
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Pseudomonas putida
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Rattus norvegicus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Rhodobacter capsulatus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Streptomyces cyanogenus
Application (protein specific)
EC Number
Application
Commentary
Organism
1.17.1.4
biotechnology
the enzyme can be useful in biotechnlogical applications requiring special conditions, e.g. extreme pH values
Acinetobacter baumannii
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Acinetobacter baumannii
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Arabidopsis thaliana
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Arthrobacter luteolus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Bos taurus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Clostridium cylindrosporum
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Drosophila melanogaster
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Enterobacter cloacae
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Gallus gallus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Homo sapiens
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Micrococcus sp.
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Ovis aries
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Pseudomonas putida
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Rattus norvegicus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Rhodobacter capsulatus
1.17.1.4
environmental protection
XDHs can find applications in environmental degradation of pollutants like aldehydes and industrial application in nucleoside drugs like ribavirin
Streptomyces cyanogenus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Arthrobacter luteolus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Bos taurus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Clostridium cylindrosporum
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Drosophila melanogaster
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Enterobacter cloacae
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Gallus gallus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Homo sapiens
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Micrococcus sp.
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Ovis aries
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Pseudomonas putida
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis
Streptomyces cyanogenus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
Acinetobacter baumannii
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
Escherichia coli
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
Rhodobacter capsulatus
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
Arabidopsis thaliana
1.17.1.4
gene xdh, sequence comparisons and phylogenetic analysis, recombinant expression of liver XDH in insect cell system
Rattus norvegicus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Acinetobacter baumannii
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Acinetobacter phage Ab105-3phi
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Arabidopsis thaliana
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Arthrobacter luteolus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Bos taurus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Clostridium cylindrosporum
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Drosophila melanogaster
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Enterobacter cloacae
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Escherichia coli
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Gallus gallus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Homo sapiens
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Micrococcus sp.
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Ovis aries
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Pseudomonas putida
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Rattus norvegicus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Rhodobacter capsulatus
1.17.1.4
FAD
a molybdenum-containing flavoprotein
Streptomyces cyanogenus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Acinetobacter baumannii
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Acinetobacter phage Ab105-3phi
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Arabidopsis thaliana
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Arthrobacter luteolus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Bos taurus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Clostridium cylindrosporum
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Drosophila melanogaster
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Enterobacter cloacae
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Escherichia coli
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Gallus gallus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Homo sapiens
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Micrococcus sp.
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Ovis aries
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Pseudomonas putida
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Rattus norvegicus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Rhodobacter capsulatus
1.17.1.4
molybdenum cofactor
a molybdenum-containing flavoprotein
Streptomyces cyanogenus
1.17.1.4
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
1.17.1.4
additional information
cofactor domain amino acid sequence comparisons, overview
Acinetobacter phage Ab105-3phi
1.17.1.4
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
1.17.1.4
additional information
cofactor domain amino acid sequence comparisons, overview
Arthrobacter luteolus
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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.
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
NAD+
-
Acinetobacter baumannii
1.17.1.4
NAD+
-
Acinetobacter phage Ab105-3phi
1.17.1.4
NAD+
-
Arthrobacter luteolus
1.17.1.4
NAD+
-
Bos taurus
1.17.1.4
NAD+
-
Clostridium cylindrosporum
1.17.1.4
NAD+
-
Drosophila melanogaster
1.17.1.4
NAD+
-
Enterobacter cloacae
1.17.1.4
NAD+
-
Escherichia coli
1.17.1.4
NAD+
-
Gallus gallus
1.17.1.4
NAD+
-
Homo sapiens
1.17.1.4
NAD+
-
Micrococcus sp.
1.17.1.4
NAD+
-
Ovis aries
1.17.1.4
NAD+
-
Pseudomonas putida
1.17.1.4
NAD+
-
Rattus norvegicus
1.17.1.4
NAD+
-
Rhodobacter capsulatus
1.17.1.4
NAD+
-
Streptomyces cyanogenus
1.17.1.4
NAD+
-
Arabidopsis thaliana
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Acinetobacter baumannii
1.17.1.4
[2Fe-2S]-center
-
Acinetobacter phage Ab105-3phi
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Arabidopsis thaliana
1.17.1.4
[2Fe-2S]-center
-
Arthrobacter luteolus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Bos taurus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Clostridium cylindrosporum
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Drosophila melanogaster
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Enterobacter cloacae
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Escherichia coli
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Gallus gallus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Homo sapiens
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Micrococcus sp.
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Ovis aries
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Pseudomonas putida
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Rattus norvegicus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Rhodobacter capsulatus
1.17.1.4
[2Fe-2S]-center
XDH consists of 3 redox center domains, one of which contains 2 distinct iron-sulfur clusters ([2Fe-2S])
Streptomyces cyanogenus
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.17.1.4
crystal structure determination
Bos taurus
1.17.1.4
crystal structure determination
Homo sapiens
1.17.1.4
crystal structure determination
Rattus norvegicus
1.17.1.4
crystal structure determination
Rhodobacter capsulatus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.17.1.4
extracellular
-
Bos taurus
-
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.17.1.4
Fe2+
in the [2Fe-2S] center
Acinetobacter baumannii
1.17.1.4
Fe2+
in the [2Fe-2S] center
Acinetobacter phage Ab105-3phi
1.17.1.4
Fe2+
in the [2Fe-2S] center
Arabidopsis thaliana
1.17.1.4
Fe2+
in the [2Fe-2S] center
Arthrobacter luteolus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Bos taurus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Clostridium cylindrosporum
1.17.1.4
Fe2+
in the [2Fe-2S] center
Drosophila melanogaster
1.17.1.4
Fe2+
in the [2Fe-2S] center
Enterobacter cloacae
1.17.1.4
Fe2+
in the [2Fe-2S] center
Escherichia coli
1.17.1.4
Fe2+
in the [2Fe-2S] center
Gallus gallus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Homo sapiens
1.17.1.4
Fe2+
in the [2Fe-2S] center
Micrococcus sp.
1.17.1.4
Fe2+
in the [2Fe-2S] center
Ovis aries
1.17.1.4
Fe2+
in the [2Fe-2S] center
Pseudomonas putida
1.17.1.4
Fe2+
in the [2Fe-2S] center
Rattus norvegicus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Rhodobacter capsulatus
1.17.1.4
Fe2+
in the [2Fe-2S] center
Streptomyces cyanogenus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Acinetobacter baumannii
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Acinetobacter phage Ab105-3phi
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein, biosynthesis of sulfurated molybdenum cofactor, overview
Arabidopsis thaliana
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Arthrobacter luteolus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Bos taurus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Clostridium cylindrosporum
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Drosophila melanogaster
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Enterobacter cloacae
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Escherichia coli
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Gallus gallus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Homo sapiens
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Micrococcus sp.
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Ovis aries
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Pseudomonas putida
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Rattus norvegicus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Rhodobacter capsulatus
1.17.1.4
Molybdenum
a molybdenum-containing flavoprotein
Streptomyces cyanogenus
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.17.1.4
128000
-
-
Enterobacter cloacae
1.17.1.4
160000
-
-
Arthrobacter luteolus
1.17.1.4
160000
-
-
Escherichia coli
1.17.1.4
270000
-
-
Rhodobacter capsulatus
1.17.1.4
290000
-
-
Acinetobacter baumannii
1.17.1.4
290000
-
-
Bos taurus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.17.1.4
xanthine + NAD+ + H2O
Gallus gallus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Drosophila melanogaster
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Homo sapiens
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Rattus norvegicus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Bos taurus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Ovis aries
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Enterobacter cloacae
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Pseudomonas putida
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Rhodobacter capsulatus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Clostridium cylindrosporum
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Micrococcus sp.
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Acinetobacter baumannii
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Streptomyces cyanogenus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Arabidopsis thaliana
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Escherichia coli
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Acinetobacter phage Ab105-3phi
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Arthrobacter luteolus
-
urate + NADH + H+
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
Rhodobacter capsulatus B10XDHB
-
urate + NADH + H+
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.17.1.4
native enzyme
Enterobacter cloacae
1.17.1.4
purification of native enzyme
Arthrobacter luteolus
1.17.1.4
purification of native XDH
Clostridium cylindrosporum
1.17.1.4
purification of native XDH
Drosophila melanogaster
1.17.1.4
purification of native XDH
Gallus gallus
1.17.1.4
purification of native XDH
Homo sapiens
1.17.1.4
purification of native XDH
Micrococcus sp.
1.17.1.4
purification of native XDH
Ovis aries
1.17.1.4
purification of native XDH
Rattus norvegicus
1.17.1.4
purification of native XDH
Rhodobacter capsulatus
1.17.1.4
purification of native XDH
Streptomyces cyanogenus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.17.1.4
liver
-
Rattus norvegicus
-
1.17.1.4
milk
-
Bos taurus
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
1.17.1.4
1.8
-
purified native enzyme, pH and temperature not specified in the publication
Bos taurus
1.17.1.4
7
-
purified recombinant enzyme, pH and temperature not specified in the publication
Escherichia coli
1.17.1.4
7.5
-
purified native enzyme, pH and temperature not specified in the publication
Enterobacter cloacae
1.17.1.4
10
-
purified native enzyme, pH and temperature not specified in the publication
Arthrobacter luteolus
1.17.1.4
17.5
-
purified enzyme, pH and temperature not specified in the publication
Rhodobacter capsulatus
1.17.1.4
29.1
-
purified recombinant enzyme, pH and temperature not specified in the publication
Acinetobacter baumannii
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.17.1.4
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
744450
Gallus gallus
?
-
-
-
-
1.17.1.4
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
744450
Drosophila melanogaster
?
-
-
-
-
1.17.1.4
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
744450
Homo sapiens
?
-
-
-
-
1.17.1.4
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
744450
Rattus norvegicus
?
-
-
-
-
1.17.1.4
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
744450
Bos taurus
?
-
-
-
-
1.17.1.4
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
744450
Ovis aries
?
-
-
-
-
1.17.1.4
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
744450
Enterobacter cloacae
?
-
-
-
-
1.17.1.4
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
744450
Pseudomonas putida
?
-
-
-
-
1.17.1.4
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
744450
Rhodobacter capsulatus
?
-
-
-
-
1.17.1.4
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
744450
Clostridium cylindrosporum
?
-
-
-
-
1.17.1.4
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
744450
Micrococcus sp.
?
-
-
-
-
1.17.1.4
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
744450
Acinetobacter baumannii
?
-
-
-
-
1.17.1.4
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
744450
Streptomyces cyanogenus
?
-
-
-
-
1.17.1.4
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
744450
Arabidopsis thaliana
?
-
-
-
-
1.17.1.4
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
744450
Escherichia coli
?
-
-
-
-
1.17.1.4
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
744450
Acinetobacter phage Ab105-3phi
?
-
-
-
-
1.17.1.4
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
744450
Arthrobacter luteolus
?
-
-
-
-
1.17.1.4
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
744450
Rhodobacter capsulatus B10XDHB
?
-
-
-
-
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Gallus gallus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Drosophila melanogaster
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Homo sapiens
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Rattus norvegicus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Bos taurus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Ovis aries
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Enterobacter cloacae
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Pseudomonas putida
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Rhodobacter capsulatus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Clostridium cylindrosporum
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Micrococcus sp.
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Acinetobacter baumannii
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Streptomyces cyanogenus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Arabidopsis thaliana
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Escherichia coli
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Acinetobacter phage Ab105-3phi
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Arthrobacter luteolus
urate + NADH + H+
-
-
-
?
1.17.1.4
xanthine + NAD+ + H2O
-
744450
Rhodobacter capsulatus B10XDHB
urate + NADH + H+
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.17.1.4
homodimer
the enzyme exists as (alpha)2 form
Arabidopsis thaliana
1.17.1.4
homodimer
2 * 80000, (alpha)2
Arthrobacter luteolus
1.17.1.4
homodimer
2 * 145000, the enzyme exists as (alpha)2 form
Bos taurus
1.17.1.4
homodimer
2 * 69000
Enterobacter cloacae
1.17.1.4
homodimer
the enzyme exists as (alpha)2 form
Gallus gallus
1.17.1.4
homodimer
the enzyme exists as (alpha)2 form
Rattus norvegicus
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
tetramer
2 * 87000, alpha-subunit, + 2 * 56000, beta-subunit, alpha2beta2
Acinetobacter baumannii
1.17.1.4
tetramer
2 * 50000, alpha-subunit, + 2 * 80000, beta-subunit, alpha2beta2
Rhodobacter capsulatus
Temperature Optimum [░C] (protein specific)
EC Number
Temperature Optimum [░C]
Temperature Optimum Maximum [░C]
Commentary
Organism
1.17.1.4
25
35
-
Bos taurus
1.17.1.4
35
40
-
Rhodobacter capsulatus
1.17.1.4
35
45
-
Enterobacter cloacae
1.17.1.4
55
60
-
Arthrobacter luteolus
1.17.1.4
65
-
-
Escherichia coli
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.17.1.4
25
-
xanthine
pH and temperature not specified in the publication
Acinetobacter baumannii
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.17.1.4
6.5
7.5
-
Enterobacter cloacae
1.17.1.4
7.5
8
-
Arthrobacter luteolus
1.17.1.4
7.5
8
-
Escherichia coli
1.17.1.4
7.5
8.5
-
Rhodobacter capsulatus
1.17.1.4
8.5
9
-
Acinetobacter baumannii
1.17.1.4
8.5
-
-
Bos taurus
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.17.1.4
additional information
-
Acinetobacter baumannii XDH extends the pH tolerance to pH 11.0
Acinetobacter baumannii
General Information
EC Number
General Information
Commentary
Organism
1.17.1.4
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
1.17.1.4
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
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Arabidopsis thaliana
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Arthrobacter luteolus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Bos taurus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Clostridium cylindrosporum
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Drosophila melanogaster
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Enterobacter cloacae
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Escherichia coli
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Gallus gallus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Homo sapiens
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Micrococcus sp.
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Ovis aries
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Pseudomonas putida
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Rattus norvegicus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Rhodobacter capsulatus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Streptomyces cyanogenus
1.17.1.4
additional information
the Arabidopsis thaliana XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
Arabidopsis thaliana
1.17.1.4
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
1.17.1.4
additional information
the chicken XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
Gallus gallus
1.17.1.4
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
1.17.1.4
additional information
the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
Rhodobacter capsulatus
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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.
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.17.1.4
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
1.17.1.4
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
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Arabidopsis thaliana
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Arthrobacter luteolus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Bos taurus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Clostridium cylindrosporum
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Drosophila melanogaster
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Enterobacter cloacae
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Escherichia coli
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Gallus gallus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Homo sapiens
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Micrococcus sp.
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Ovis aries
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Pseudomonas putida
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Rattus norvegicus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Rhodobacter capsulatus
1.17.1.4
evolution
XDHs are widely distributed in all eukarya, bacteria and archaea domains, phylogenetic analysis
Streptomyces cyanogenus
1.17.1.4
additional information
the Arabidopsis thaliana XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
Arabidopsis thaliana
1.17.1.4
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
1.17.1.4
additional information
the chicken XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
Gallus gallus
1.17.1.4
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
1.17.1.4
additional information
the Rhodobacter capsulatus XDH cannot be converted to oxidase form by neither proteolytic cleavage nor oxidation of specific cysteine residues
Rhodobacter capsulatus
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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.
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
1.17.1.4
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
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.17.1.4
2740
-
xanthine
pH and temperature not specified in the publication
Acinetobacter baumannii
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.17.1.4
2740
-
xanthine
pH and temperature not specified in the publication
Acinetobacter baumannii