Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
tRNAn+1 + phosphate | Escherichia coli | the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability | tRNAn + a nucleoside diphosphate | - |
? | |
tRNAn+1 + phosphate | Escherichia coli MG1655 | the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability | tRNAn + a nucleoside diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli MG1655 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
tRNAn+1 + phosphate | the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability | Escherichia coli | tRNAn + a nucleoside diphosphate | - |
? | |
tRNAn+1 + phosphate | the enzyme is a 3' to 5' RNase. RNase PH uses phosphate as a nucleophile to catalyze RNA cleavage | Escherichia coli | tRNAn + a nucleoside diphosphate | - |
? | |
tRNAn+1 + phosphate | the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability | Escherichia coli MG1655 | tRNAn + a nucleoside diphosphate | - |
? | |
tRNAn+1 + phosphate | the enzyme is a 3' to 5' RNase. RNase PH uses phosphate as a nucleophile to catalyze RNA cleavage | Escherichia coli MG1655 | tRNAn + a nucleoside diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RNase PH | - |
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 | - |
assay at | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
malfunction | absence of RNase PH and polynucleotide phosphorylase, EC 2.7.7.8, causes growth defects. Absence of both enzymes results in the appearance and accumulation of novel mRNA degradation fragments, which are also observed in strains containing mutations in RNase R and PNPase, enzymes whose collective absence is known to cause an accumulation of structured RNA fragments. Single or double deletion of either pnp or rph had a moderate effect on the rpsO, trxA, or lpp mRNAs | Escherichia coli |
physiological function | role for RNase PH in the degradation of structured RNA, overview | Escherichia coli |