Literature summary for 3.1.26.5 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.

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Protein Variants

Protein Variants	Comment	Organism
E40C	site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme	Bacillus subtilis
Y113C	site-directed mutagenesis, comparison of metal effects on enzyme-substrate complex formation with the wild-type enzyme	Bacillus subtilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics and kinetic mechanism of reaction and enzyme stablization with metal ions, overview	Bacillus subtilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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
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
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Bacillus subtilis	the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
ribonucleoprotein	ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme catalyzes the 5' end maturation of precursor tRNAs (pre-tRNAs)	Bacillus subtilis	?	-	?
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	?	-	?
pre-tRNA + H2O	-	Bacillus subtilis	tRNA + 5' leader of tRNA	-	?
pre-tRNAAsp + H2O	5' fluorescein-labeled Bacillus subtilis pre-tRNAAsp (Fl-pre-tRNA) possessing a 5-nucleotide leader	Bacillus subtilis	?	-	?

Subunits

Subunits	Comment	Organism
More	ribonuclease P is composed of a catalytically active RNA (PRNA) and a small protein (P protein) subunit	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
RNase P	-	Bacillus subtilis

General Information

General Information	Comment	Organism
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
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
physiological function	the enzyme catalyzes the 5' end maturation of precursor tRNAs	Bacillus subtilis

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Release 2023.1 (January 2023)