3.1.26.7: ribonuclease P4
This is an abbreviated version!
For detailed information about ribonuclease P4, go to the full flat file.
Reaction
endonucleolytic cleavage of RNA, removing 3'-extranucleotides from tRNA precursor =
Synonyms
P4, ribonuclease P ribozyme, ribonuclease P RNA, RNase P, RNase P RNA, RNaseP P4
ECTree
3.1.26.7 ribonuclease P4Advanced search results
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results (Metals Ions
Metals Ions on EC 3.1.26.7 - ribonuclease P4
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
-
preferred by mutant ribozyme, binding structure of the enzyme RNA P4 element, affinities of wild-type and mutant P4 element
Mg2+
additional information
-
conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of the ribozyme
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
Mg2+
-
25 mM, required for folding and catalytic function, metal binding site and coordination study using site-specific phosphorothioate substitutions, helix P4: the pro-Sp phosphate of Ala67 is involved in metal ion positioning
Mg2+
-
preferred by wild-type ribozyme, binding structure of the enzyme RNA P4 element, affinities of wild-type and mutant P4 element
Mg2+
-
required, potential metal binding sites identification by Tb3+ cleavage
