EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.26.5 | E40C | site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme | Bacillus subtilis |
3.1.26.5 | Y113C | site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.26.5 | additional information | - |
additional information | kinetics and kinetic mechanism of reaction and enzyme stablization with metal ions, overview | Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.26.5 | Ca2+ | a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. Structural changes that occur upon binding Ca(II) to the ES complex are determined by time-resolved FRET measurements of the distances between donor/acceptor fluorophores introduced at specific locations on the P protein and pre-tRNA 5' leader. The value of KD,obs has an apparent hyperbolic dependence on the concentration of calcium with an apparent dissociation constant for Ca(II) of 0.04 mM | Bacillus subtilis | |
3.1.26.5 | Mg2+ | a divalent cation stabilizes the active conformation of the RNase P-pre-tRNA complex, a role for an inner-sphere metal ion, Mg2+ or Ca2+, in the enzyme. A second, lower affinity Mg(II) activates cleavage catalyzed by the enzyme | Bacillus subtilis | |
3.1.26.5 | additional information | catalysis of pre-tRNA cleavage by RNase P requires at least one divalent cation capable of forming inner-sphere coordination, such as Mg2+, Mn2+, Zn2+ or Ca2+ | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.26.5 | additional information | Bacillus subtilis | the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs) | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.26.5 | Bacillus subtilis | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.26.5 | ribonucleoprotein | ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit | Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.26.5 | additional information | the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs) | Bacillus subtilis | ? | - |
? | |
3.1.26.5 | additional information | the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs). Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P-pre-tRNA complex, which undergoes an essential conformational change before the cleavage step | Bacillus subtilis | ? | - |
? | |
3.1.26.5 | pre-tRNA + H2O | - |
Bacillus subtilis | tRNA + 5' leader of tRNA | - |
? | |
3.1.26.5 | pre-tRNAAsp + H2O | 5' fluorescein-labeled Bacillus subtilis pre-tRNAAsp (Fl-pre-tRNA) possessing a 5-nucleotide leader | Bacillus subtilis | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.26.5 | More | ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit | Bacillus subtilis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.26.5 | RNase P | - |
Bacillus subtilis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.26.5 | additional information | the metal-dependent conformational change re-organizes the bound substrate in the active site to form a catalytically competent RNase P-pre-tRNA complex | Bacillus subtilis |
3.1.26.5 | physiological function | Bacillus subtilis RNase P, composed of a catalytically active RNA, PRNA, and a small protein, the P protein, subunit, catalyzes the 5' end maturation of precursor tRNAs. Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P/pre-tRNA complex. Previous studies have demonstrated that this RNase P/pre-tRNA complex undergoes an essential conformational change before the cleavage step. The RNase P/pre-tRNA conformer is stabilized by a high affinity divalent cation capable of inner-sphere coordination, such as Ca2+ or Mg2+. A second, lower affinity Mg2+ activates cleavage catalyzed by RNase P. Conformational changes and structural analysis, overview | Bacillus subtilis |
3.1.26.5 | physiological function | the enzyme catalyzes the 5' end maturation of precursor tRNAs | Bacillus subtilis |