Crystallization (Comment) | Organism |
---|---|
RihA bound to inhibitor 3,4-diaminophenyl-D-iminoribitol, hanging drop vapour diffusion method, 8 mg/ml RihA in 50 mM HEPES, pH 7.2, 150 mM NaCl is mixed with a 5:1 molar excess of 3,4-diaminophenyl-D-iminoribitol, solubilized in 50 mM HEPES, pH 7.2, and incubated at 4°C for 3 hours, the protein/inhibitor complex is mixed with an equal volume of a precipitant solution containing 25% PEG 4000, 0.1 M sodium acetate, pH 5.0, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3,4-diaminophenyl-D-iminoribitol | competitive, the ligand can bind at the active site in two distinct orientations, binding structure, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | dependent on | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a pyrimidine nucleoside + H2O | Escherichia coli | - |
D-ribose + a pyrimidine base | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a pyrimidine nucleoside + H2O | - |
Escherichia coli | D-ribose + a pyrimidine base | - |
? | |
additional information | catalytic cycles between the open and closed conformations of RihA, stabilization of two flexible active site regions is pivotal to establish the interactions required for substrate discrimination and catalysis, involvement of the Asp10 as general base in the mechanism, role of the conserved His82 residue in modulating product release, structure-function analysis, detailed overview | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
More | the enzyme belongs to the pyrimidine-preferring N-ribohydrolases, CU-NHs, a class of Ca2+-dependent enzymes that catalyze the hydrolytic cleavage of the N-glycosidic bond in pyrimidine nucleosides | Escherichia coli |
N-ribohydrolase | - |
Escherichia coli |
RihA | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.085 | - |
3,4-diaminophenyl-D-iminoribitol | pH 7.4, 37°C | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | possible role of CU-NHs in the breakdown of modified nucleosides derived from RNA molecules | Escherichia coli |