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Literature summary for 3.1.26.7 extracted from

  • Getz, M.M.; Andrews, A.J.; Fierke, C.A.; Al-Hashimi, H.M.
    Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation (2007), RNA, 13, 251-266.
    View publication on PubMedView publication on EuropePMC
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Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ catalytically important metal, presence of 15-20 mM Mg2+ does not significantly alter structure or dynamics of the P4 element, metal binding seems to be involved in substrate binding rather than in conformational changes Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pre-tRNA + H2O Bacillus subtilis involved in the hydrolysis of phosphodiester bonds in precursors of transfer RNA (pre-tRNA) to form mature tRNA tRNA + pre-part nucleotides
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Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNA + H2O involved in the hydrolysis of phosphodiester bonds in precursors of transfer RNA (pre-tRNA) to form mature tRNA Bacillus subtilis tRNA + pre-part nucleotides
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 ?

Synonyms

Synonyms Comment Organism
RNaseP P4 the P4 helix is an essential element of ribonuclease P (RNase P) Bacillus subtilis