Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystal structures of the wild type in complexes with phosphate and sulfate, respectively, and of the R24A mutant in complex with phosphate/sulfate, to about 2 A resolution. The structural data show that previously observed conformational change is a result of the phosphate binding and its interaction with residue Arg24 | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D204A | 0.1% of wild-type activity towards inosine, adenosine and guanosine | Escherichia coli |
D204A/R217A | about 0.2% of wild-type activity towards inosine, adenosine and guanosine | Escherichia coli |
D204N | less than about 4% of wild-type activity towards inosine, adenosine and guanosine | Escherichia coli |
R217A | about 0.5% of wild-type activity towards inosine and guanosine, 10.8% of activity towards adenosine | Escherichia coli |
R24A | absence of a conformational change upon binding of phosphate, about 0.2 to 0.6% of wild-type activity towards inosine, adenosine and guanosine | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0ABP8 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.041 | - |
substrate inosine, mutant R217A, pH 7.0, 25°C | Escherichia coli |
0.05 | - |
substrate adenosine, mutant D204A, pH 7.0, 25°C | Escherichia coli |
0.06 | - |
substrate guanosine, mutant D204A, pH 7.0, 25°C | Escherichia coli |
0.07 | - |
substrate adenosine, mutant D204N, pH 7.0, 25°C | Escherichia coli |
0.07 | - |
substrate guanosine, mutant D204A/R217A, pH 7.0, 25°C | Escherichia coli |
0.09 | - |
substrate guanosine, mutant R24A, pH 7.0, 25°C | Escherichia coli |
0.09 | - |
substrate inosine, mutant D204A, pH 7.0, 25°C | Escherichia coli |
0.13 | - |
substrate adenosine, mutant D204A/R217A, pH 7.0, 25°C | Escherichia coli |
0.14 | - |
substrate inosine, mutant D204A/R217A, pH 7.0, 25°C | Escherichia coli |
0.18 | - |
substrate inosine, mutant R24A, pH 7.0, 25°C | Escherichia coli |
0.36 | - |
substrate adenosine, mutant R24A, pH 7.0, 25°C | Escherichia coli |
0.36 | - |
substrate guanosine, mutant R217A, pH 7.0, 25°C | Escherichia coli |
1.4 | - |
substrate inosine, mutant D204N, pH 7.0, 25°C | Escherichia coli |
2.1 | - |
substrate guanosine, mutant D204N, pH 7.0, 25°C | Escherichia coli |
6.3 | - |
substrate adenosine, mutant R217A, pH 7.0, 25°C | Escherichia coli |
6.4 | - |
substrate 7-methylguanosine, mutant R24A, pH 7.0, 25°C | Escherichia coli |
6.9 | - |
substrate 7-methylguanosine, mutant D204N, pH 7.0, 25°C | Escherichia coli |
20 | - |
substrate 7-methylguanosine, mutant D204A, pH 7.0, 25°C | Escherichia coli |
21.3 | - |
substrate 7-methylguanosine, mutant R217A, pH 7.0, 25°C | Escherichia coli |
21.4 | - |
substrate 7-methylguanosine, wild-type, pH 7.0, 25°C | Escherichia coli |
46.9 | - |
substrate 7-methylguanosine, mutant D204A/R217A, pH 7.0, 25°C | Escherichia coli |
58.5 | - |
substrate adenosine, wild-type, pH 7.0, 25°C | Escherichia coli |
60.4 | - |
substrate guanosine, wild-type, pH 7.0, 25°C | Escherichia coli |
103.2 | - |
substrate inosine, wild-type, pH 7.0, 25°C | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
7-methylguanosine + phosphate | - |
Escherichia coli | 7-methylguanine + alpha-D-ribose 1-phosphate | - |
? | |
adenosine + phosphate | - |
Escherichia coli | adenine + alpha-D-ribose 1-phosphate | - |
? | |
guanosine + phosphate | - |
Escherichia coli | guanine + alpha-D-ribose 1-phosphate | - |
? | |
inosine + phosphate | - |
Escherichia coli | hypoxanthine + alpha-D-ribose 1-phosphate | - |
? | |
additional information | catalysis involves protonation of the purine base at position N7 by residue Asp204, which is triggered by Arg217 | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DeoD | - |
Escherichia coli |