EC Number |
Title |
Organism |
---|
3.1.26.7 | Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA |
Escherichia coli |
3.1.26.7 | Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme |
Escherichia coli |
3.1.26.7 | Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid precursor |
Escherichia coli |
3.1.26.7 | Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid precursor |
Escherichia coli MRE 600 |
3.1.26.7 | Solution structure and metal-ion binding of the P4 element from bacterial RNase P RNA |
Escherichia coli |
3.1.26.7 | Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation |
Bacillus subtilis |
3.1.26.7 | Total synthesis of a tyrosine suppressor transfer RNA gene. XVII. Transcription, in vitro, of the synthetic gene and processing of the primary transcript to transfer RNA |
Escherichia coli |
3.1.26.7 | Total synthesis of a tyrosine suppressor transfer RNA gene. XVII. Transcription, in vitro, of the synthetic gene and processing of the primary transcript to transfer RNA |
Escherichia coli MRE 600 |