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Literature summary extracted from
- Ribonuclease P: a ribonucleoprotein enzyme (2000), Curr. Opin. Chem. Biol., 4, 553-558.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.26.5 | 3 possible RNA-binding motifs, including a putative single-stranded RNA-binding cleft formed by an alpha-helix and a four-stranded beta-sheet, derived from crystal structure and NMR study | Staphylococcus aureus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.5 | additional information | substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold | Bacillus subtilis | |
| 3.1.26.5 | additional information | substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold | Escherichia coli | |
| 3.1.26.5 | additional information | substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold | Staphylococcus aureus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.5 | Mg2+ | potential catalytic transition state structure including 3 required divalent metal ions, coordinated to nonbinding phosphate group oxygens | Bacillus subtilis |  |
| 3.1.26.5 | Mg2+ | potential catalytic transition state structure including 3 required divalent metal ions, coordinated to nonbinding phosphate group oxygens | Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.5 | Bacillus subtilis | - |
- |
- |
| 3.1.26.5 | Escherichia coli | - |
- |
- |
| 3.1.26.5 | Staphylococcus aureus | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.26.5 | ribonucleoprotein | - |
Staphylococcus aureus |
| 3.1.26.5 | ribonucleoprotein | - |
Bacillus subtilis |
| 3.1.26.5 | ribonucleoprotein | - |
Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.1.26.5 | endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor | an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules structure-function study, substrate recognition and catalytic mechanism of the ribozyme | Bacillus subtilis | |
| 3.1.26.5 | endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor | an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules structure-function study, substrate recognition and catalytic mechanism of the ribozyme | Escherichia coli | |
| 3.1.26.5 | endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor | an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, structure-function study, substrate recognition and catalytic mechanism of the ribozyme | Staphylococcus aureus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.5 | additional information | substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold | Staphylococcus aureus | ? | - |
? | |
| 3.1.26.5 | additional information | substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold | Bacillus subtilis | ? | - |
? | |
| 3.1.26.5 | additional information | substitution of a sulfur atom for either the Rp or Sp nonbridging phosphate oxygen or the 3'oxyanion leaving group in pre-tRNA decreases the catalytic rate constant by over 1000fold | Escherichia coli | ? | - |
? | |
| 3.1.26.5 | tRNAAsp precursor + H2O | sequence | Staphylococcus aureus | mature tRNAAsp + 5'-terminal oligonucleotide | 5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl | ir | |
| 3.1.26.5 | tRNAAsp precursor + H2O | sequence | Bacillus subtilis | mature tRNAAsp + 5'-terminal oligonucleotide | 5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl | ir | |
| 3.1.26.5 | tRNAAsp precursor + H2O | sequence, potential catalytic transition state structure including 3 required divalent metal ions | Escherichia coli | mature tRNAAsp + 5'-terminal oligonucleotide | 5'-terminal oligonucleotide with 3'-hydroxyl and 5'-phosphoryl | ir | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.5 | More | primary and secondary structure of the ribozymal RNA, catalytic domain and specificity domain, structure of the ribozyme plays an important role in catalysis, overview | Bacillus subtilis |
| 3.1.26.5 | More | primary and secondary structure of the ribozymal RNA, catalytic domain and specificity domain, structure of the ribozyme plays an important role in catalysis, overview | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.5 | RNase P | - |
Staphylococcus aureus |
| 3.1.26.5 | RNase P | - |
Bacillus subtilis |
| 3.1.26.5 | RNase P | - |
Escherichia coli |
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