Application | Comment | Organism |
---|---|---|
medicine | observed only in microorganisms, target for antimicrobial drug | Aspergillus clavatus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli HMS174 cells | Aspergillus clavatus |
Protein Variants | Comment | Organism |
---|---|---|
D153A | mutation without affecting substrate binding but critical role in catalysis, decrease in catalytic proficiency | Aspergillus clavatus |
E73A | mutation with affect on substrate binding, decrease in catalytic proficiency | Aspergillus clavatus |
K353A | mutation without affecting substrate binding but critical role in catalysis, decrease in catalytic proficiency | Aspergillus clavatus |
R155A | mutation with affect on substrate binding, decrease in catalytic proficiency | Aspergillus clavatus |
Y152A | mutation with affect on substrate binding, decrease in catalytic proficiency | Aspergillus clavatus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.025 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | wild-type enzyme | Aspergillus clavatus | |
0.04 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant D153A | Aspergillus clavatus | |
0.14 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant E73A | Aspergillus clavatus | |
0.18 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant R155A | Aspergillus clavatus | |
0.46 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant Y152A | Aspergillus clavatus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus clavatus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
standard methods with nickel nitrilotiacetic acid resin | Aspergillus clavatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO3- | assay at pH 7.5, 37°C | Aspergillus clavatus | ADP + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
N5-CAIR synthetase | - |
Aspergillus clavatus |
N5-carboxyaminoimidazole ribonucleotide synthetase | - |
Aspergillus clavatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Aspergillus clavatus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Aspergillus clavatus |
General Information | Comment | Organism |
---|---|---|
physiological function | key enzyme in microbial de novo purine biosynthesis | Aspergillus clavatus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.67 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant E73A | Aspergillus clavatus | |
2 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant D153A | Aspergillus clavatus | |
8.3 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant Y152A | Aspergillus clavatus | |
100 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | mutant R155A | Aspergillus clavatus | |
5500 | - |
5-amino-1-(5-phospho-D-ribosyl)imidazole | wild-type enzyme | Aspergillus clavatus |