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Literature summary for 3.1.26.5 extracted from

  • Wu, S.; Kikovska, E.; Lindell, M.; Kirsebom, L.A.
    Cleavage mediated by the catalytic domain of bacterial RNase P RNA (2012), J. Mol. Biol., 422, 204-214.
    View publication on PubMed
Search for more literature for 3.1.26.5

Protein Variants

Protein Variants Comment Organism
additional information seperation of the catalytic domain of the RNA part by cleaving it from the specificity S-domain mediates. Compared to full-length RNase P RNA, the rate constant, kobs, of cleavage of various model RNA hairpin loop substrates.for the truncated RPR is reduced 30 to 13000fold depending on the substrate. Substitution of A248, positioned near the cleavage site in the RNase P-substrate complex, with G in the truncated RNase P RNA results in 30fold improvement in reaction rate. In contrast, strengthening the interaction between the RNase P RNA and the 3'-end of the substrate only had a modest effect. Deleting the S-domain gives a reduction in the rate, but it results in a less erroneous RPR with respect to cleavage site selection Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, the requirement of Mg2+ for catalysis varies with the substrate. Deletion of the S-domain changes the Mg2+ requirement Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli precursor tRNAs are natural enzyme RNase P substrates ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
ribonucleoprotein the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information precursor tRNAs are natural enzyme RNase P substrates Escherichia coli ?
-
 ?
additional information usage of model hairpin loop RNA substrates, e.g. pMini3bpUG, pATSerCG or pATSerUG, secondary structures, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions Escherichia coli

Synonyms

Synonyms Comment Organism
RNase P
-
 Escherichia coli

General Information

General Information Comment Organism
malfunction deletion of the S-domain reduces the activity rate, changes the Mg2+ requirement, and has a significant impact on the kinetic of cleavage for substrates carrying C-1/G+73. Substitutions in the truncated mutant, e.g. at pposition 248, can partly compensate for the absence of the S-domain, overview Escherichia coli
additional information the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions, the structural architecture of the -1/+73 plays a significant role where a C-1/G+73 pair has the most dramatic effect on kobs Escherichia coli