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Literature summary for 4.6.1.19 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

Cloned(Commentary)

Cloned (Comment) Organism
RNase P is a ribonucleoprotein consisting of a large RNA and protein components, RNA P4 helix samples are prepared by in vitro transcription reactions Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Synonyms

Synonyms Comment Organism
ribonuclease P
-
Bacillus subtilis
RNase P
-
Bacillus subtilis