Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.5 extracted from

  • Cuzic-Feltens, S.; Weber, M.H.; Hartmann, R.K.
    Investigation of catalysis by bacterial RNase P via LNA and other modifications at the scissile phosphodiester (2009), Nucleic Acids Res., 37, 7638-7653.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Cloned(Commentary)

Cloned (Comment) Organism
N-terminal His-tagged RNase P protein overexpressed Bacillus subtilis
N-terminal His-tagged RNase P protein overexpressed Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ presence of the protein cofactor increases and equalized substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA Escherichia coli
Ca2+ presence of the protein cofactor increases and equalizes substrate affinity and abolishes the substrate affinity differences seen for Escherichia coli relative to Bacillus subtilis P RNA Bacillus subtilis
Mg2+ required for catalysis Bacillus subtilis
Mg2+ for the LNA variant, parallel pathways leading to cleavage at the c0 and m+1 sites have different pH profiles, with a higher Mg2+ requirement for c0 versus m+1 cleavage. The strong catalytic defect for LNA and 2'-OCH3 supports a model where the extra methylene (LNA) or methyl group (2'-OCH3) causes a steric interference with a nearby bound catalytic Mg2+ during its recoordination on the way to the transition state for cleavage. Presence of the protein cofactor suppresses the ground state binding defects, but not the catalytic defects Escherichia coli

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
precursor tRNA + H2O cleavage of precursor tRNAs with an LNA (extra methylene), 2'-OCH3, 2'-H or 2'-F modification at the canonical (c0) site by type A RNase P RNA. Extent of cleavage for the LNA (T-1) and 2'-OCH3 (T-1) substrates is extremely low. LNA and 2'-OCH3 suppress processing at the major aberrant m-1 site. Instead, the m+1 (nt +1/+2) site is utilized Escherichia coli ?
-
 ?
precursor tRNA + H2O cleavage of precursor tRNAs with an LNA (extra methylene), 2'-OCH3, 2'-H or 2'-F modification at the canonical (c0) site by type B RNase P RNA. Extent of cleavage for the LNA (T-1) and 2'-OCH3 (T-1) substrates is extremely low. Weak cleavage of the 2'-OCH3 substrate at the c0 site. Stronger defect caused by 2'-H at nt -1 as compared to the Escherichia coli holoenzyme Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
ribonuclease P
-
 Bacillus subtilis
ribonuclease P
-
 Escherichia coli
RNase P
-
 Bacillus subtilis
RNase P
-
 Escherichia coli
RNase P RNA
-
 Bacillus subtilis
RNase P RNA
-
 Escherichia coli