Protein Variants | Comment | Organism |
---|---|---|
Q157A | is a conserved glutamine in the Aa-RNase III dsRNA-binding domain. Aa-RNase III cleavage of the pre-16S substrate is blocked by the Q157A mutation, which reflects a loss of substrate binding affinity. But the Q157A mutation does not affect folding or structure in a significant manner | Aquifex aeolicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
KCl | activates at 50 mM, inhibits at concentrations above 100 mM | Aquifex aeolicus | |
NaCl | activates at 50 mM, inhibits at concentrations above 100 mM | Aquifex aeolicus | |
NH4Cl | activates at 50 mM, inhibits at concentrations above 100 mM | Aquifex aeolicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Aquifex aeolicus | |
0.00098 | - |
Aa-[16S[micro-hp]RNA] | pH 8.0, 40°C | Aquifex aeolicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | activates at 50 mM, inhibits at concentrations above 100 mM | Aquifex aeolicus | |
Mg2+ | required, Mg2+ and Mn2+ both support the catalytic reaction | Aquifex aeolicus | |
Mn2+ | required, Mg2+ and Mn2+ both support the catalytic reaction | Aquifex aeolicus | |
additional information | no activation by Ni2+, Co2+, and Ca2+ | Aquifex aeolicus | |
NaCl | activates at 50 mM, inhibits at concentrations above 100 mM | Aquifex aeolicus | |
NH4Cl | activates at 50 mM, inhibits at concentrations above 100 mM | Aquifex aeolicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Aquifex aeolicus | small hairpins based on the stem structures associated with the Aquifex 16S and 23S rRNA precursors are cleaved at sites that are consistent with production of the immediate precursors to the mature rRNAs. Substrate reactivity is independent of the distal box sequence, but is strongly dependent on the proximal box sequence. RNase III mechanism of dsRNA cleavage, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Aa-[16S[micro-hp]RNA] + H2O | structures of the Aquifex pre-16S and pre-23S rRNA processing stems and corresponding hairpin substrates, overview | Aquifex aeolicus | ? | - |
? | |
additional information | small hairpins based on the stem structures associated with the Aquifex 16S and 23S rRNA precursors are cleaved at sites that are consistent with production of the immediate precursors to the mature rRNAs. Substrate reactivity is independent of the distal box sequence, but is strongly dependent on the proximal box sequence. RNase III mechanism of dsRNA cleavage, overview | Aquifex aeolicus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease III | - |
Aquifex aeolicus |
RNase III | - |
Aquifex aeolicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | 85 | - |
Aquifex aeolicus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 85 | and above, activity range | Aquifex aeolicus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 85 | Aa-RNase III activity increases from 35°C, reaching a maximum at 70°C, and shows significant activity up to 85°C | Aquifex aeolicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.045 | - |
Aa-[16S[micro-hp]RNA] | pH 8.0, 40°C | Aquifex aeolicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 9 | broad maximum | Aquifex aeolicus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 9 | and above, activity range | Aquifex aeolicus |
General Information | Comment | Organism |
---|---|---|
additional information | Q157 is a conserved glutamine in the Aa-RNase III dsRNA-binding domain | Aquifex aeolicus |
physiological function | ribonuclease III cleaves double-stranded structures in bacterial RNAs and participates in diverse RNA maturation and decay pathways, RNase III mechanism of dsRNA cleavage, overview | Aquifex aeolicus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
466.7 | - |
Aa-[16S[micro-hp]RNA] | pH 8.0, 40°C | Aquifex aeolicus |