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Literature summary for 3.1.26.5 extracted from

  • Sharin, E.; Schein, A.; Mann, H.; Ben-Asouli, Y.; Jarrous, N.
    RNase P: role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis (2005), Nucleic Acids Res., 33, 5120-5132.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information
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Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information the protein component C5 acts as a cofactor for the catalytic M1 RNA subunit that processes the 5' leader sequence of precursor tRNA. Rpp29, a conserved protein subunit of human RNase P, can substitute for C5 protein in reconstitution assay of M1 RNA activity. Distinct protein folds in two unrelated protein cofactors can facilitate transition from RNA-based to ribonucleoprotein-based catalysis by RNase P Escherichia coli