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Literature summary extracted from

  • Hsieh, J.; Koutmou, K.S.; Rueda, D.; Koutmos, M.; Walter, N.G.; Fierke, C.A.
    A divalent cation stabilizes the active conformation of the B. subtilis RNase P x pre-tRNA complex: a role for an inner-sphere metal ion in RNase P (2010), J. Mol. Biol., 400, 38-51.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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) ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Bacillus subtilis
-
-
-

Posttranslational Modification

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

Substrates and Products (Substrate)

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 ?
-
?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 RNase P
-
Bacillus subtilis

General Information

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