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Literature summary for 3.1.26.5 extracted from

  • Kirsebom, L.A.; Trobro, S.
    RNase P RNA-mediated cleavage (2009), IUBMB Life, 61, 189-200.
    View publication on PubMed
Search for more literature for 3.1.26.5

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ Ca2+ can replace Mg2+ Homo sapiens
Mg2+ enzymatic activity depends on the presence of divalent metal ions such as Mg2+ Bacillus subtilis
Mg2+ enzymatic activity depends on the presence of divalent metal ions such as Mg2+ Homo sapiens
Mg2+ enzymatic activity depends on the presence of divalent metal ions such as Mg2+ Chlamydia sp.
Mn2+ Mn2+ can replace Mg2+ Homo sapiens
Pb2+ Pb2+ can replace Mg2+ Homo sapiens
Zn2+ Zn2+ can replace Mg2+ Homo sapiens

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Chlamydia sp.
-
-
-
Homo sapiens
-
-
-
no activity in Nanoarchaeum equitans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNA precursor + H2O
-
 Bacillus subtilis tRNA + 5'-oligoribonucleotide
-
 ?
pre-tRNA precursor + H2O
-
 Homo sapiens tRNA + 5'-oligoribonucleotide
-
 ?
pre-tRNA precursor + H2O
-
 Chlamydia sp. tRNA + 5'-oligoribonucleotide
-
 ?
tRNATyrUAG precursor + H2O RNase P cleavage of this substrate generates a 5' matured tRNA with a 7 base pair amino acceptor stem Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
RNase P RNase P RNA lacks the P15-loop structure but is still capable to mediate cleavage at the canonical RNase P cleavage site Chlamydia sp.
RNase P the catalytic RNA subunit of RNase P is a trans-acting ribozyme that cleaves various RNA substrates in vitro generating 5'-phosphates and 3'-hydroxyls as cleavage products Homo sapiens
RNase P the holoenzyme consists of two RNase P RNA and two protein subunits Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
additional information RNase P RNA is capable of cleaving its substrate in vitro in the absence of any protein cofactor Homo sapiens