EC Number | Cloned (Comment) | Organism |
---|---|---|
1.17.1.4 | C-terminally His6-tagged wild-type and mutant XDHs expression in Escherichia coli strain TP1000 | Rhodobacter capsulatus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.17.1.4 | C134A/C136A | site-directed mutagenesis, an inactive subunit A mutant | Rhodobacter capsulatus |
1.17.1.4 | C44A/C47A | site-directed mutagenesis, an instable subunit A mutant that cannot be purified | Rhodobacter capsulatus |
1.17.1.4 | E220R/D517R | site-directed mutagenesis, a subunit B mutant that is mainly dimeris incontrast to the tetrameric wild-type enzyme, inactive mutant | Rhodobacter capsulatus |
1.17.1.4 | Q102A | site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme | Rhodobacter capsulatus |
1.17.1.4 | Q102G | site-directed mutagenesis, a subunit A mutant that shows altered metal content and reduced KM and Kcat with xanthine compared to the wild-type enzyme | Rhodobacter capsulatus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.17.1.4 | 0.0227 | - |
xanthine | pH 7.8, 25°C, mutant Q102G, with NAD+ | Rhodobacter capsulatus | |
1.17.1.4 | 0.0293 | - |
xanthine | pH 7.8, 25°C, mutant Q102A, with NAD+ | Rhodobacter capsulatus | |
1.17.1.4 | 0.0328 | - |
NAD+ | pH 7.8, 25°C, wild-type enzyme | Rhodobacter capsulatus | |
1.17.1.4 | 0.0373 | - |
NAD+ | pH 7.8, 25°C, mutant Q102G | Rhodobacter capsulatus | |
1.17.1.4 | 0.0402 | - |
NAD+ | pH 7.8, 25°C, mutant Q102A | Rhodobacter capsulatus | |
1.17.1.4 | 0.0442 | - |
xanthine | pH 7.8, 25°C, wild-type enzyme, with NAD+ | Rhodobacter capsulatus | |
1.17.1.4 | 0.0809 | - |
DCPIP | pH 7.8, 25°C, mutants Q102A and Q102G | Rhodobacter capsulatus | |
1.17.1.4 | 0.0823 | - |
DCPIP | pH 7.8, 25°C, wild-type enzyme | Rhodobacter capsulatus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | Iron | the enzyme is a molybdo-flavoprotein, the enzyme tetramer contains two [2Fe-2S] clusters | Rhodobacter capsulatus | |
1.17.1.4 | Molybdenum | the enzyme is molybdo-flavoprotein, one cofactor molecule per enzyme tetramer | Rhodobacter capsulatus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.4 | xanthine + NAD+ + H2O | Rhodobacter capsulatus | - |
urate + NADH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.1.4 | Rhodobacter capsulatus | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.17.1.4 | flavoprotein | - |
Rhodobacter capsulatus |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.17.1.4 | recombinant His-tagged wild-type and mutant XDHs from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by ultrafiltration and gel filtration | Rhodobacter capsulatus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.4 | xanthine + DCIP + H2O | - |
Rhodobacter capsulatus | urate + reduced DCIP | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | - |
Rhodobacter capsulatus | urate + NADH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.17.1.4 | heterotetramer | (alphabeta)2 structure, mechanism of assembly and cofactor insertion on two different polypeptides: dimerization of the (alphabeta) subunits has to precede molybdenum cofactor insertion, the two subunits act independently without cooperativity, incomplete assembly of FeSI impairs the formation of the XDH (alphabeta)2 heterotetramer and, thus, insertion of the molybdenum cofactor into the enzyme, overview | Rhodobacter capsulatus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.17.1.4 | XDH | - |
Rhodobacter capsulatus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.17.1.4 | 25 | - |
assay at | Rhodobacter capsulatus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.17.1.4 | 31.6 | - |
xanthine | pH 7.8, 25°C, mutant Q102G, with DCIP | Rhodobacter capsulatus | |
1.17.1.4 | 34.3 | - |
xanthine | pH 7.8, 25°C, mutant Q102A, with DCIP | Rhodobacter capsulatus | |
1.17.1.4 | 39.5 | - |
xanthine | pH 7.8, 25°C, mutant Q102A, with NAD+ | Rhodobacter capsulatus | |
1.17.1.4 | 40.6 | - |
xanthine | pH 7.8, 25°C, mutant Q102G, with NAD+ | Rhodobacter capsulatus | |
1.17.1.4 | 66.1 | - |
xanthine | pH 7.8, 25°C, wild-type enzyme, with DCIP | Rhodobacter capsulatus | |
1.17.1.4 | 77.5 | - |
xanthine | pH 7.8, 25°C, wild-type enzyme, with NAD+ | Rhodobacter capsulatus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.17.1.4 | 7.5 | 7.8 | assay at | Rhodobacter capsulatus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | molybdenum cofactor | binding involves residues GluB730, GlnA102, CysA103, CysA106, CysA134, and CysA13 of the alpha and beta subunits | Rhodobacter capsulatus | |
1.17.1.4 | NAD+ | - |
Rhodobacter capsulatus | |
1.17.1.4 | [2Fe-2S] cluster | - |
Rhodobacter capsulatus |