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Literature summary for 3.1.26.5 extracted from

  • Guerrier-Takada, C.; van Belkum, A.; Pleij, C.W.A.; Altman, S.
    Novel reactions of RNAase P with a tRNA-like structure in turnip yellow mosaic virus RNA (1988), Cell, 53, 267-272.
    View publication on PubMed
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KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pre-tRNA + H2O Escherichia coli in addition to its essential role in the biosynthesis of tRNA, RNase P may have another function in vivo, namely, in the physiology of viral infections tRNA + 5'-oligoribonucleotide
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNA + H2O in addition to its essential role in the biosynthesis of tRNA, RNase P may have another function in vivo, namely, in the physiology of viral infections Escherichia coli tRNA + 5'-oligoribonucleotide
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 ?
pre-tRNA precursor + H2O M1 RNA alone and the RNAse P holoenzyme from E. coli cleave the tRNA-like structure of TYMV RNA in vitro at the 5'-side of the quasi-helical structure to generate 5'-phosphate and 3'-hydroxyl groups in the cleavage products. The intact pseudoknot structure in the substrate is not required for the reaction catalyzed by M1 RNA alone, but its presence markedly improves the efficiency of the reaction Escherichia coli tRNA + 5'-oligoribonucleotide
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 ?

Turnover Number [1/s]

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